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PDBsum entry 4l4v
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Membrane protein/immune system
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PDB id
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4l4v
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Contents |
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262 a.a.
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99 a.a.
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200 a.a.
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243 a.a.
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188 a.a.
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PDB id:
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| Name: |
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Membrane protein/immune system
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Title:
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Structure of human mait tcr in complex with human mr1-rl-6-me-7-oh
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Structure:
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Major histocompatibility complex class i-related gene protein. Chain: a, c. Fragment: extracellular domain, residues 23-292. Engineered: yes. Mutation: yes. Beta-2-microglobulin. Chain: b, f. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mr1. Expressed in: escherichia coli. Expression_system_taxid: 511693. Gene: b2m. Gene: tcr alpha. Gene: tcr beta.
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Resolution:
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1.90Å
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R-factor:
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0.179
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R-free:
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0.209
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Authors:
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O.Patel,L.Kjer-Nielsen,J.Le Nours,S.B.G.Eckle,R.W.Birkinshaw, T.Beddoe,A.J.Corbett,L.Liu,J.J.Miles,B.Meehan,R.Reantragoon, M.L.Sandoval-Romero,L.C.Sullivan,A.G.Brooks,Z.Chen,D.P.Fairlie, J.Mccluskey,J.Rossjohn
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Key ref:
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O.Patel
et al.
(2013).
Recognition of vitamin B metabolites by mucosal-associated invariant T cells.
Nat Commun,
4,
2142.
PubMed id:
DOI:
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Date:
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09-Jun-13
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Release date:
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17-Jul-13
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PROCHECK
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Headers
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References
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Q95460
(HMR1_HUMAN) -
Major histocompatibility complex class I-related gene protein from Homo sapiens
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Seq: Struc:
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341 a.a.
262 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.
99 a.a.
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Q6P4G7
(Q6P4G7_HUMAN) -
TRA@ protein from Homo sapiens
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Seq: Struc:
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260 a.a.
200 a.a.*
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DOI no:
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Nat Commun
4:2142
(2013)
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PubMed id:
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Recognition of vitamin B metabolites by mucosal-associated invariant T cells.
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O.Patel,
L.Kjer-Nielsen,
J.Le Nours,
S.B.Eckle,
R.Birkinshaw,
T.Beddoe,
A.J.Corbett,
L.Liu,
J.J.Miles,
B.Meehan,
R.Reantragoon,
M.L.Sandoval-Romero,
L.C.Sullivan,
A.G.Brooks,
Z.Chen,
D.P.Fairlie,
J.McCluskey,
J.Rossjohn.
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ABSTRACT
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The mucosal-associated invariant T-cell antigen receptor (MAIT TCR) recognizes
MR1 presenting vitamin B metabolites. Here we describe the structures of a human
MAIT TCR in complex with human MR1 presenting a non-stimulatory ligand derived
from folic acid and an agonist ligand derived from a riboflavin metabolite. For
both vitamin B antigens, the MAIT TCR docks in a conserved manner above MR1,
thus acting as an innate-like pattern recognition receptor. The invariant MAIT
TCR α-chain usage is attributable to MR1-mediated interactions that prise open
the MR1 cleft to allow contact with the vitamin B metabolite. Although the
non-stimulatory antigen does not contact the MAIT TCR, the stimulatory antigen
does. This results in a higher affinity of the MAIT TCR for a stimulatory
antigen in comparison with a non-stimulatory antigen. We formally demonstrate a
structural basis for MAIT TCR recognition of vitamin B metabolites, while
illuminating how TCRs recognize microbial metabolic signatures.
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');
}
}
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