PDBsum entry 4mq7

Immune system

PDB id: 4mq7

Contents

Protein chains

268 a.a.

98 a.a.

Ligands

NAG

CIS

Waters ×85

PDB id:

4mq7

Name:

Immune system

Title:

Structure of human cd1d-sulfatide

Structure:

Antigen-presenting glycoprotein cd1d, cd1d1 protein. Chain: a. Fragment: human cd1d alpha1,2 domains fused with murine alpha3 domain. Synonym: r3g1. Engineered: yes. Mutation: yes. Beta-2-microglobulin. Chain: b.

Source:

Homo sapiens, mus musculus. Human, mouse. Organism_taxid: 9606, 10090. Gene: cd1d, cd1.2, cd1d1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Mus musculus. Mouse. Organism_taxid: 10090.

Resolution:

2.60Å R-factor: 0.224 R-free: 0.284

Authors:

A.M.Luoma,E.J.Adams

Key ref:

A.M.Luoma et al. (2013). Crystal structure of Vδ1 T cell receptor in complex with CD1d-sulfatide shows MHC-like recognition of a self-lipid by human γδ T cells. Immunity, 39, 1032-1042. PubMed id: 24239091 DOI: 10.1016/j.immuni.2013.11.001

Date:

15-Sep-13 Release date: 18-Dec-13

Protein chain

P11609  (CD1D1_MOUSE) -  Antigen-presenting glycoprotein CD1d1 from Mus musculus

Seq: 336 a.a.

Struc: 268 a.a.*

Protein chain

P15813  (CD1D_HUMAN) -  Antigen-presenting glycoprotein CD1d from Homo sapiens

Seq: 335 a.a.

Struc: 268 a.a.*

Protein chain

P01887  (B2MG_MOUSE) -  Beta-2-microglobulin from Mus musculus

Seq: 119 a.a.

Struc: 98 a.a.

* PDB and UniProt seqs differ at 92 residue positions (black crosses)

DOI no: 10.1016/j.immuni.2013.11.001

Immunity 39:1032-1042 (2013)

PubMed id: 24239091

Crystal structure of Vδ1 T cell receptor in complex with CD1d-sulfatide shows MHC-like recognition of a self-lipid by human γδ T cells.

A.M.Luoma, C.D.Castro, T.Mayassi, L.A.Bembinster, L.Bai, D.Picard, B.Anderson, L.Scharf, J.E.Kung, L.V.Sibener, P.B.Savage, B.Jabri, A.Bendelac, E.J.Adams.

ABSTRACT

The nature of the antigens recognized by γδ T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vδ1 TCR-expressing γδ T cells, the major γδ lymphocyte population in epithelial tissues. We crystallized a Vδ1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vδ1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3δ residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vδ1+ γδ T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ T cells and reveal the prevalence of lipid recognition by innate-like T cell populations.