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8ZHR

Cryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3A2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001817biological_processregulation of cytokine production
A0005102molecular_functionsignaling receptor binding
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0009897cellular_componentexternal side of plasma membrane
A0016020cellular_componentmembrane
A0050852biological_processT cell receptor signaling pathway
B0001817biological_processregulation of cytokine production
B0005102molecular_functionsignaling receptor binding
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0009897cellular_componentexternal side of plasma membrane
B0016020cellular_componentmembrane
B0050852biological_processT cell receptor signaling pathway
E0001817biological_processregulation of cytokine production
E0002250biological_processadaptive immune response
E0002376biological_processimmune system process
E0002456biological_processT cell mediated immunity
E0005102molecular_functionsignaling receptor binding
E0005515molecular_functionprotein binding
E0005886cellular_componentplasma membrane
E0009897cellular_componentexternal side of plasma membrane
E0016020cellular_componentmembrane
E0032729biological_processpositive regulation of type II interferon production
E0050852biological_processT cell receptor signaling pathway
F0001817biological_processregulation of cytokine production
F0001819biological_processpositive regulation of cytokine production
F0002250biological_processadaptive immune response
F0002376biological_processimmune system process
F0005102molecular_functionsignaling receptor binding
F0005515molecular_functionprotein binding
F0005886cellular_componentplasma membrane
F0009897cellular_componentexternal side of plasma membrane
F0032729biological_processpositive regulation of type II interferon production
F0050798biological_processactivated T cell proliferation
F0050852biological_processT cell receptor signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues880
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues333
DetailsDomain: {"description":"Ig-like V-type"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues47
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues583
DetailsDomain: {"description":"B30.2/SPRY","evidences":[{"source":"PROSITE-ProRule","id":"PRU00548","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues241
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues109
DetailsDomain: {"description":"Ig-like V-type 1"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues91
DetailsDomain: {"description":"Ig-like V-type 2"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22846996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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