Family Search for PF09291 (DUF1968)

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PF09291 hits 60 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.

P01849 T-cell receptor alpha chain constant from Mus musculus
Aligns to 6:86 / 136 (59.6%), covers 100.0% of PF09291, 135.5 bits

• SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice.
  Shen, Scientific reports 2016
  • “...this Research Article is as the follows: T cell receptor alpha chain, P01848 (human) and P01849 (mouse); SARS-CoV, P59594; HIV-1, P04578. How to cite this article : Shen, Z. T. and Sigalov, A. B. SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice. Sci....”
• Disruption of IL-21 signaling affects T cell-B cell interactions and abrogates protective humoral immunity to malaria
  Pérez-Mazliah, PLoS pathogens 2015
  • “...T-cell receptor alpha chain C region [ Mus musculus ]; Gene ID: 21473; Uniprot ID: P01849 Rag2 V(D)J recombination-activating protein 2 [ Mus musculus ]; Gene ID: 19374; UniProt ID: P21784 Il21 Interleukin-21 [ Mus musculus ]; Gene ID: 60505; Uniprot ID: Q9ES17 Il21r Interleukin-21 receptor...”

A2NTU7 Cytotoxic Tcell receptor from Mus musculus
Aligns to 138:218 / 268 (30.2%), covers 100.0% of PF09291, 132.8 bits

• Activating interactions of sulfanilamides with T cell receptors.
  Watkins, Open journal of immunology 2013
  • “...second control, we used a single TCR and from an M. musculis found in Uniprot A2NTU7 and Q7TND8, with models generated as described. Sequences are shown in supplemental Table 1 for all reactive clones used to generate initial models. All were aligned to the closest matching...”

TRAC_HUMAN / P01848 T cell receptor alpha chain constant from Homo sapiens (Human) (see 2 papers)
Aligns to 6:90 / 140 (60.7%), covers 91.4% of PF09291, 130.4 bits

• function: Constant region of T cell receptor (TR) alpha chain (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen- activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa- B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post- thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585).
  subunit: Alpha-beta TR is a heterodimer composed of an alpha and beta chain; disulfide-linked. The alpha-beta TR is associated with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TcR or TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in the endoplasmic reticulum where a single alpha-beta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 homodimer forming a stable octameric structure. CD3D-CD3E and CD3G-CD3E heterodimers preferentially associate with TR alpha and TR beta chains, respectively. The association of the CD247 homodimer is the last step of TcR assembly in the endoplasmic reticulum and is required for transport to the cell surface.
• A TCR-like CAR Promotes Sensitive Antigen Recognition and Controlled T-cell Expansion Upon mRNA Vaccination.
  Birtel, Cancer research communications 2022
  • “...An artificial disulfide bond between C and C was introduced at position hTRAC T47C (Uniprot: P01848) or mTRAC T48C (UniProt: A0A075B662) and hTRBC S57C (UniProt: P01850) or mTRBC [UniProt: A0A075B5J4 ( 26 )]. For the incorporation into retroviral backbones, both the CLDN6- and CLDN18.2-TCAR chains were...”
• The Full Model of the pMHC-TCR-CD3 Complex: A Structural and Dynamical Characterization of Bound and Unbound States.
  Alba, Cells 2022
  • “...], using the sequences as provided by the Uniprot database [ 32 ] (Uniprot entries P01848 and P01850 for the TCR and chains, respectively; Q9MY51 for the chain of the HLA-A*02:01). The resulting complexes were assembled, solvated with the TIP3P water model and minimized using GROMACS...”
• Molecular Dynamics Simulations Reveal Canonical Conformations in Different pMHC/TCR Interactions.
  Alba, Cells 2020
  • “...following the amino acid sequences provided by the Uniprot database [ 12 ] (Uniprot entries P01848 and P01850 for the TCR and chains respectively; Q9MY51 for the chain of the HLA-A* 02:01). The heterogeneous lipid bilayer was built by means of the CHARMM-GUI Membrane Builder web...”
• SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice
  Shen, Scientific reports 2016
  • “...sequences discussed in this Research Article is as the follows: T cell receptor alpha chain, P01848 (human) and P01849 (mouse); SARS-CoV, P59594; HIV-1, P04578. How to cite this article : Shen, Z. T. and Sigalov, A. B. SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in...”

2ckbA / P01738 Structure of the 2c/kb/dev8 complex (see paper)
Aligns to 118:198 / 202 (40.1%), covers 100.0% of PF09291, 129.4 bits

• Ligand: peptide (2ckbA)

7phrA Structure of a fully assembled t-cell receptor engaging a tumor- associated peptide-mhc i (see paper)
Aligns to 109:193 / 243 (35.0%), covers 91.4% of PF09291, 128.9 bits

• Ligand: peptide (7phrA)

7fjem / A0A0B4J271,A0N4Z6,P01848 Cryo-em structure of a membrane protein(ll) (see paper)
Aligns to 112:196 / 246 (34.6%), covers 91.4% of PF09291, 128.8 bits

• Ligand: peptide (7fjem)

3kprD / P01848 Crystal structure of the lc13 tcr in complex with hla b 4405 Bound to eeylkawtf a mimotope (see paper)
Aligns to 118:201 / 201 (41.8%), covers 91.4% of PF09291, 128.5 bits

• Ligand: peptide (3kprD)

1ogaD / P01848 A structural basis for immunodominant human t-cell receptor recognition. (see paper)
Aligns to 116:199 / 199 (42.2%), covers 91.4% of PF09291, 128.4 bits

• Ligand: peptide (1ogaD)

TRAR1_HUMAN / P0DSE1 M1-specific T cell receptor alpha chain; TR alpha chain TRAV27*01J42*01C*01 from Homo sapiens (Human) (see 6 papers)
Aligns to 134:218 / 268 (31.7%), covers 91.4% of PF09291, 128.4 bits

• function: The alpha chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA- A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TR clonotype, it is preferentially selected in effector memory CD8-positive T cells among multiple HLA-A*02:01 carriers and confers long-lived immunity against IAV infection. Can cross-recognize sporadically emerging IAV variants by molecular mimicry, inducing immunity toward different influenza strains (PubMed:1833769, PubMed:7807026, PubMed:29997621, PubMed:27036003, PubMed:12796775, PubMed:18275829). Antigen recognition initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell differentiation into effector/memory T cells (By similarity).
  subunit: Disulfide-linked heterodimer with TRBV19*01J2S7*01C*02 beta chain. The TR primarily interacts via its CDR3-beta domain with M/matrix protein 1-derived peptide (GILGFVFTL) displayed by HLA-A*02.01 in a 'peg-notch' recognition mode (PubMed:27036003, PubMed:12796775, PubMed:18275829). The alpha-beta TR associates with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in the endoplasmic reticulum where a single alpha-beta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 homodimer forming a stable octameric structure. CD3D-CD3E and CD3G-CD3E heterodimers preferentially associate with TR alpha and TR beta chains (via TM domain), respectively. The association of the CD247 homodimer is the last step of TCR assembly in the endoplasmic reticulum and is required for transport to the cell surface (By similarity).

2j8uE / P01849 Large cdr3a loop alteration as a function of mhc mutation. (see paper)
Aligns to 121:194 / 194 (38.1%), covers 90.1% of PF09291, 127.6 bits

• Ligand: peptide (2j8uE)

TRAR2_HUMAN / P0DTU3 T cell receptor alpha chain MC.7.G5; MC.7.G5 TRA; TR alpha chain TRAV38-2DV8*01J31*01C*01 from Homo sapiens (Human) (see paper)
Aligns to 141:225 / 275 (30.9%), covers 91.4% of PF09291, 127.6 bits

• function: The alpha chain of TRAV38-2DV8*01J31*01C*01/TRBV25- 1*01J2S3*01C2*01 alpha-beta T cell receptor (TR) clonotype that displays pan-cancer cell recognition via the invariant MR1 molecule. On CD8-positive T cell clone MC.7.G5, likely recognizes tumor-specific or -associated metabolite(s) essential for cancer cell survival, triggering killing of many cancer cell types including lung, melanoma, leukemia, colon, breast, prostate, bone and ovarian cancer cells. Mediates cancer cell cytotoxicity in an HLA-independent manner. Has no reactivity to healthy cells, even stressed or infected by bacteria (PubMed:31959982). Antigen recognition initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell differentiation into effector/memory T cells (By similarity).
  subunit: Disulfide-linked heterodimer with TRBV25-1*01J2S3*01C2*01 beta chain (PubMed:31959982). The alpha-beta TR associates with the transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in the endoplasmic reticulum where a single alpha-beta TR heterodimer associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer and one CD247 homodimer forming a stable octameric structure. CD3D-CD3E and CD3G-CD3E heterodimers preferentially associate with TR alpha and TR beta chains (via TM domain), respectively. The association of the CD247 homodimer is the last step of TCR assembly in the endoplasmic reticulum and is required for transport to the cell surface (By similarity).

8gvgA The complex between public tcr td08 and hla-a24 bound to HIV-1 nef138- 8 (2f) peptide (see paper)
Aligns to 120:203 / 203 (41.4%), covers 91.4% of PF09291, 127.2 bits

• Ligand: peptide (8gvgA)

Q5I0I7 RGD1359684 protein from Rattus norvegicus
Aligns to 137:216 / 266 (30.1%), covers 98.8% of PF09291, 126.5 bits

• Prenatal Stress Impairs Postnatal Learning and Memory Development via Disturbance of the cGMP-PKG Pathway and Oxidative Phosphorylation in the Hippocampus of Rats.
  Li, Frontiers in molecular neuroscience 2020
  • “...1 (Vdac1) Q63014 A-kinase anchoring protein 8 (Akap8) Q03346 Peptidase, mitochondrial processing beta subunit (Pmpcb) Q5I0I7 Similar to T cell receptor V-alpha J-alpha (LOC290071) TABLE 2 Downregulated proteins in the hippocampus of pups. Accession Protein names Q9Z270 VAMP-associated protein A (Vapa) Q6PCU0 ATP synthase, H+ transporting,...”

7m72C / K7N5N2 Mhc-like protein complex structure (see paper)
Aligns to 120:204 / 204 (41.7%), covers 91.4% of PF09291, 126.1 bits

• Ligand: (3r)-n-[(2s,3r)-1-(alpha-d-galactopyranosyloxy)-3-hydroxy-15-methylhexadecan-2-yl]-3-hydroxyheptadecanamide (7m72C)

7n6eI Tcr peptide hla-a2 complex (see paper)
Aligns to 115:199 / 199 (42.7%), covers 91.4% of PF09291, 126.0 bits

• Ligand: peptide (7n6eI)

3mbeC / P01849 Tcr 21.30 in complex with mhc class ii i-ag7hel(11-27) (see paper)
Aligns to 116:192 / 192 (40.1%), covers 93.8% of PF09291, 125.9 bits

• Ligand: peptide (3mbeC)

4p2oC Crystal structure of the 2b4 tcr in complex with 2a/i-ek (see paper)
Aligns to 116:200 / 200 (42.5%), covers 91.4% of PF09291, 125.9 bits

• Ligand: peptide (4p2oC)

7rm4E Neoantigen p53r175h-specific tcr 6-11 binds to p53r175h-hla-a2 (see paper)
Aligns to 116:200 / 200 (42.5%), covers 91.4% of PF09291, 125.8 bits

• Ligand: peptide (7rm4E)

4qrpD Crystal structure of hla b 0801 In complex with hskkkcdel and dd31 tcr (see paper)
Aligns to 119:203 / 203 (41.9%), covers 91.4% of PF09291, 125.7 bits

• Ligand: peptide (4qrpD)

7n4kD / A0A075B6C4,K7N5N2 6218 tcr in complex with h2-db pa 224 (see paper)
Aligns to 115:199 / 199 (42.7%), covers 91.4% of PF09291, 125.7 bits

• Ligand: peptide (7n4kD)

3w0wD The complex between t36-5 tcr and hla-a24 bound to HIV-1 nef134-10(2f) peptide in space group p212121 (see paper)
Aligns to 117:201 / 204 (41.7%), covers 91.4% of PF09291, 125.7 bits

• Ligand: peptide (3w0wD)

7n1eD Sars-cov-2 rlq peptide-specific tcr prlq3 binds to rlq-hla-a2 (see paper)
Aligns to 117:200 / 200 (42.0%), covers 91.4% of PF09291, 125.6 bits

• Ligand: peptide (7n1eD)

5tezI Tcr f50 recgonizing m1-hla-a2 (see paper)
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.5 bits

• Ligand: peptide (5tezI)

4prhD / P01848 Crystal structure of tk3 tcr-hla-b 35:08-Hpvg-d5 complex (see paper)
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.3 bits

• Ligand: peptide (4prhD)

6vmxD Structure of hd14 tcr in complex with hla-b7 presenting an ebv epitope (see paper)
Aligns to 120:203 / 203 (41.4%), covers 91.4% of PF09291, 125.3 bits

• Ligand: peptide (6vmxD)

6avfA / A0A0B4J268 Crystal structure of the kfj5 tcr-ny-eso-1-hla-b 07:02 Complex (see paper)
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.2 bits

• Ligand: peptide (6avfA)

5wkfI / A0A087WSZ9,K7N5N2 D30 tcr in complex with hla-a 11:01-Gts1 (see paper)
Aligns to 115:198 / 198 (42.4%), covers 91.4% of PF09291, 125.2 bits

• Ligand: peptide (5wkfI)

4g8gD Crystal structure of c12c tcr-ha b2705-kk10 (see paper)
Aligns to 121:204 / 204 (41.2%), covers 91.4% of PF09291, 125.2 bits

• Ligand: peptide (4g8gD)

8cx4D Tcr-antigen complex as8.4-yeih-hla B27 (see paper)
Aligns to 123:206 / 206 (40.8%), covers 91.4% of PF09291, 125.2 bits

• Ligand: peptide (8cx4D)

5menD / A0A0B4J277,K7N5M3 Human leukocyte antigen a02 presenting ilakflhwl, in complex with cognate t-cell receptor (see paper)
Aligns to 117:200 / 200 (42.0%), covers 91.4% of PF09291, 125.2 bits

• Ligand: peptide (5menD)

5w1vI Structure of the hla-e-vmaprtlil/gf4 tcr complex (see paper)
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.1 bits

• Ligand: peptide (5w1vI)

8d5qA Tcr tg6 in complex with ld-hf10 (see paper)
Aligns to 122:205 / 205 (41.0%), covers 91.4% of PF09291, 125.1 bits

• Ligand: peptide (8d5qA)

2po6G / P01848 Crystal structure of cd1d-lipid-antigen complexed with beta-2- microglobulin, nkt15 alpha-chain and nkt15 beta-chain (see paper)
Aligns to 120:204 / 204 (41.7%), covers 91.4% of PF09291, 125.1 bits

• Ligand: n-{(1s,2r,3s)-1-[(alpha-d-galactopyranosyloxy)methyl]-2,3-dihydroxyheptadecyl}hexacosanamide (2po6G)

6r0eDDD 6r0eDDD (see paper)
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.0 bits

• Ligand: peptide (6r0eDDD)

6v18D Immune receptor complex (see paper)
Aligns to 122:206 / 206 (41.3%), covers 91.4% of PF09291, 125.0 bits

• Ligand: peptide (6v18D)

5jziD Crystal structure of 1406 tcr bound to hla-a2 with hcv 1406-1415 antigen peptide (see paper)
Aligns to 123:207 / 207 (41.1%), covers 91.4% of PF09291, 125.0 bits

• Ligand: peptide (5jziD)

7dznE Crystal structure of the cross-restricted t18a tcr and hlab4201 bound to HIV-1 gag tl9 peptide
Aligns to 119:202 / 202 (41.6%), covers 91.4% of PF09291, 125.0 bits

• Ligand: peptide (7dznE)

Q3SZN6 T cell receptor, alpha from Bos taurus
Aligns to 134:218 / 268 (31.7%), covers 98.8% of PF09291, 125.0 bits

• Impact of chronic alcohol ingestion on cardiac muscle protein expression.
  Fogle, Alcoholism, clinical and experimental research 2010
  • “...Tmed10 Q63584 NP_445919.1 0.02 Tmp21 TMEDA T-cell receptor alpha chain TRA Q569B0 RGD1359684 0.47 Q561R6 Q3SZN6 Parathyroid hormone 2 receptor Pth2r Q91V95 NP_644676.1 0.48 Pthr2 uc007bhu.1 Low-density lipoprotein receptor-related protein 2 Lrp2 P98158 NP_110454.1 0.41 T42737 Table 6 Effect of Chronic Alcohol Consumption on Cytosolic Proteins...”

5ivxE Crystal structure of b4.2.3 t-cell receptor and h2-dd p18-i10 complex (see paper)
Aligns to 120:194 / 194 (38.7%), covers 91.4% of PF09291, 124.7 bits

• Ligand: peptide (5ivxE)

3tpuC 42f3 p5e8/h2-ld complex (see paper)
Aligns to 121:204 / 204 (41.2%), covers 91.4% of PF09291, 124.5 bits

• Ligand: peptide (3tpuC)

6dfqC Mouse diabetogenic tcr i.29 (see paper)
Aligns to 117:200 / 200 (42.0%), covers 91.4% of PF09291, 124.4 bits

• Ligand: calcium ion (6dfqC)

3rugE Crystal structure of valpha10-vbeta8.1 nkt tcr in complex with cd1d- alphaglucosylceramide (c20:2) (see paper)
Aligns to 115:198 / 198 (42.4%), covers 91.4% of PF09291, 124.4 bits

• Ligand: (11e,14e)-n-[(2s,3s,4r)-1-(alpha-d-glucopyranosyloxy)-3,4-dihydroxyoctadecan-2-yl]icosa-11,14-dienamide (3rugE)

2ak4D / P01848 Crystal structure of sb27 tcr in complex with hla-b 3508- 13Mer peptide (see paper)
Aligns to 121:204 / 204 (41.2%), covers 91.4% of PF09291, 124.4 bits

• Ligand: peptide (2ak4D)

2yplD Structural features underlying t-cell receptor sensitivity to concealed mhc class i micropolymorphisms (see paper)
Aligns to 116:199 / 199 (42.2%), covers 91.4% of PF09291, 124.4 bits

• Ligand: peptide (2yplD)

A5PK91 LOC785621 protein from Bos taurus
Aligns to 138:222 / 272 (31.2%), covers 98.8% of PF09291, 122.8 bits

• Comparative Analysis of Erythrocyte Proteomes of Water Buffalo, Dairy Cattle, and Beef Cattle by Shotgun LC-MS/MS
  Guo, Frontiers in veterinary science 2019
  • “...subunit beta type 2 2 29937 6.9 Q3MHY8 RNA-binding protein 7 1 1 29962.58 9.66 A5PK91 LOC785621 protein 1 1 29974.84 6.42 Q3T014 Bisphosphoglycerate mutase 3 3 30060.91 6.03 L8J3F4 S-methyl-5'-thioadenosine phosphorylase (Fragment) 1 1 30222.66 6.82 L8HU80 COP9 signalosome complex subunit 7a 1 1 30299.27...”

6vrnD T cell receptor-p53-hla-a2 complex (see paper)
Aligns to 117:188 / 188 (38.3%), covers 88.9% of PF09291, 120.7 bits

• Ligand: peptide (6vrnD)

6rsyI The complex between tcr a7b2 and human class i mhc hla-a0201-wt1 with the bound rmfpnapyl peptide. (see paper)
Aligns to 120:191 / 191 (37.7%), covers 88.9% of PF09291, 120.1 bits

• Ligand: peptide (6rsyI)

5l2kD Crystal structure of gem42 tcr-cd1b-gmm complex (see paper)
Aligns to 117:185 / 185 (37.3%), covers 85.2% of PF09291, 115.6 bits

• Ligand: 6-o-[(2r,3r)-3-hydroxy-2-tetradecyldocosanoyl]-alpha-l-idopyranose (5l2kD)

4qrrD Crystal structure of hla b 3501-Ips in complex with a delta-beta tcr, clone 12 tcr (see paper)
Aligns to 124:202 / 203 (38.9%), covers 91.4% of PF09291, 115.3 bits

• Ligand: peptide (4qrrD)

7z50H Structure of the highly diabetogenic 4.1-t cell receptor targeting a hybrid insulin peptide bound to i-ag7. (see paper)
Aligns to 116:186 / 186 (38.2%), covers 90.1% of PF09291, 115.2 bits

• Ligand: peptide (7z50H)

2q86C / P01849 Structure of the mouse invariant nkt cell receptor valpha14 (see paper)
Aligns to 117:190 / 190 (38.9%), covers 93.8% of PF09291, 111.0 bits

• Ligand: alpha-d-mannopyranose (2q86C)

6mssA Diversity in the type ii natural killer t cell receptor repertoire and antigen specificity leads to differing cd1d docking strategies (see paper)
Aligns to 114:181 / 181 (37.6%), covers 88.9% of PF09291, 103.0 bits

• Ligand: (2s)-2-(heptadecanoyloxy)-3-{[(10s)-10-methyloctadecanoyl]oxy}propyl alpha-d-glucopyranosiduronic acid (6mssA)

1bd2D / P01848,P04437 Complex between human t-cell receptor b7, viral peptide (tax) and mhc class i molecule hla-a 0201 (see paper)
Aligns to 117:189 / 190 (38.4%), covers 91.4% of PF09291, 98.2 bits

• Ligand: peptide (1bd2D)

7na5D Structure of the h2db-tcr ternary complex with hsf2 melanoma neoantigen
Aligns to 115:180 / 180 (36.7%), covers 90.1% of PF09291, 98.1 bits

• Ligand: peptide (7na5D)

LOC102158035 uncharacterized LOC102158035 precursor from Sus scrofa
Aligns to 135:218 / 268 (31.3%), covers 100.0% of PF09291, 97.1 bits

• Effects of Cysticercus cellulosae Excretory-Secretory Antigens on the TGF-β Signaling Pathway and Th17 Cell Differentiation in Piglets, a Proteomic Analysis
  He, Microorganisms 2023
  • “...1.207999945 Yes O02705 Heat shock protein HSP 90-alpha HSP90AA1 1.174000025 Yes A0A287BF83 DUF1968 domain-containing protein LOC102158035 1.167999983 Yes P07200 Transforming growth factor beta-1 proprotein TGF1 1.125 Yes A0A287BD27 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma PLCG1 1.093999982 Yes F1SLT4 T-cell surface antigen T4/Leu-3 CD4 1.085999966 Yes A0A287A669 Interferon regulatory...”

6rpbS Crystal structure of the t-cell receptor nye_s1 bound to hla a2 01- Sllmwitqv (see paper)
Aligns to 116:188 / 189 (38.6%), covers 91.4% of PF09291, 90.5 bits

• Ligand: peptide (6rpbS)

1zglM / P01848 Crystal structure of 3a6 tcr bound to mbp/hla-dr2a (see paper)
Aligns to 113:177 / 178 (36.5%), covers 75.3% of PF09291, 71.9 bits

• Ligand: peptide (1zglM)

4e41D Structural basis for the recognition of mutant self by a tumor- specific, mhc class ii-restricted t cell receptor g4
Aligns to 116:181 / 181 (36.5%), covers 90.1% of PF09291, 69.4 bits

• Ligand: peptide (4e41D)

4gg8E / K7N5N2 Immune receptor (see paper)
Aligns to 113:174 / 174 (35.6%), covers 64.2% of PF09291, 61.8 bits

• Ligand: alpha-d-glucopyranose (4gg8E)

6rpaD Crystal structure of the t-cell receptor nye_s2 bound to hla a2 01- Sllmwitqv (see paper)
Aligns to 124:166 / 166 (25.9%), covers 67.9% of PF09291, 36.3 bits

• Ligand: peptide (6rpaD)

Or search for genetic data about PF09291 in the Fitness Browser