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PDBsum entry 4x6d
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Immune system
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PDB id
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4x6d
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Contents |
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267 a.a.
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86 a.a.
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218 a.a.
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78 a.a.
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189 a.a.
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241 a.a.
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200 a.a.
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PDB id:
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| Name: |
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Immune system
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Title:
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Cd1a ternary complex with endogenous lipids and bk6 tcr
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Structure:
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T-cell surface glycoprotein cd1a. Chain: a, c. Synonym: t-cell surface antigen t6/leu-6,hta1 thymocyte antigen. Engineered: yes. Beta-2-microglobulin. Chain: b, d. Engineered: yes. Tcr alpha. Chain: e, g.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cd1a. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: b2m, cdabp0092, hdcma22p. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.98Å
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R-factor:
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0.180
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R-free:
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0.229
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Authors:
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R.W.Birkinshaw,J.Rossjohn
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Key ref:
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R.W.Birkinshaw
et al.
(2015).
αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
Nat Immunol,
16,
258-266.
PubMed id:
DOI:
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Date:
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08-Dec-14
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Release date:
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28-Jan-15
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PROCHECK
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Headers
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References
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P06126
(CD1A_HUMAN) -
T-cell surface glycoprotein CD1a from Homo sapiens
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Seq:
Struc:
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327 a.a.
267 a.a.*
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P61769
(B2MG_HUMAN) -
Beta-2-microglobulin from Homo sapiens
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Seq:
Struc:
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119 a.a.
86 a.a.
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P06126
(CD1A_HUMAN) -
T-cell surface glycoprotein CD1a from Homo sapiens
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Seq:
Struc:
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327 a.a.
218 a.a.*
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P61769
(B2MG_HUMAN) -
Beta-2-microglobulin from Homo sapiens
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Seq:
Struc:
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119 a.a.
78 a.a.
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P01848
(TCA_HUMAN) -
T cell receptor alpha chain constant from Homo sapiens
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Seq:
Struc:
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140 a.a.
189 a.a.*
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DOI no:
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Nat Immunol
16:258-266
(2015)
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PubMed id:
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αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
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R.W.Birkinshaw,
D.G.Pellicci,
T.Y.Cheng,
A.N.Keller,
M.Sandoval-Romero,
S.Gras,
A.de Jong,
A.P.Uldrich,
D.B.Moody,
D.I.Godfrey,
J.Rossjohn.
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ABSTRACT
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A central paradigm in αβ T cell-mediated immunity is the simultaneous
co-recognition of antigens and antigen-presenting molecules by the αβ T cell
antigen receptor (TCR). CD1a presents a broad repertoire of lipid-based
antigens. We found that a prototypical autoreactive TCR bound CD1a when it was
presenting a series of permissive endogenous ligands, while other lipid ligands
were nonpermissive to TCR binding. The structures of two TCR-CD1a-lipid
complexes showed that the TCR docked over the A' roof of CD1a in a manner that
precluded direct contact with permissive ligands. Nonpermissive ligands
indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone. The
exclusive recognition of CD1a by the TCR represents a previously unknown
mechanism whereby αβ T cells indirectly sense self antigens that are bound to
an antigen-presenting molecule.
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