PDBsum entry 2mim

Immune system

PDB id: 2mim

Contents

Protein chain

178 a.a.

PDB id:

2mim

Name:

Immune system

Title:

Nmr structure of the chicken cd3 epsilon delta/gamma heterodimer

Structure:

Cd3 epsilon protein,cd3 glycoprotein. Chain: a. Fragment: chicken cd3 epsilon domain (unp residues 24-91),chicken cd3 gamma-delta domain (unp residues 18-97). Synonym: cd3e protein,cd3d antigen delta,cd3g/d protein. Engineered: yes. Other_details: chimera of cd3 epsilon protein, linker, cd3 glycoprotein

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: cd3 epsilon, cd3e, cd3g, cd3d, d. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

S.Headey,R.Berry,J.Rossjohn

Key ref:

R.Berry et al. (2014). Structure of the chicken CD3εδ/γ heterodimer and its assembly with the αβT cell receptor. J Biol Chem, 289, 8240-8251. PubMed id: 24488493 DOI: 10.1074/jbc.M113.544965

Date:

15-Dec-13 Release date: 12-Feb-14

Protein chain

P70069  (P70069_CHICK) -  T-cell surface glycoprotein CD3 epsilon chain from Gallus gallus

Seq: 175 a.a.

Struc: 178 a.a.*

Protein chain

Q90768  (Q90768_CHICK) -  CD3 glycoprotein from Gallus gallus

Seq: 175 a.a.

Struc: 178 a.a.*

* PDB and UniProt seqs differ at 100 residue positions (black crosses)

DOI no: 10.1074/jbc.M113.544965

J Biol Chem 289:8240-8251 (2014)

PubMed id: 24488493

Structure of the chicken CD3εδ/γ heterodimer and its assembly with the αβT cell receptor.

R.Berry, S.J.Headey, M.J.Call, J.McCluskey, C.A.Tregaskes, J.Kaufman, R.Koh, M.J.Scanlon, M.E.Call, J.Rossjohn.

ABSTRACT

In mammals, the αβT cell receptor (TCR) signaling complex is composed of a TCRαβ heterodimer that is noncovalently coupled to three dimeric signaling molecules, CD3εδ, CD3εγ, and CD3ζζ. The nature of the TCR signaling complex and subunit arrangement in different species remains unclear however. Here we present a structural and biochemical analysis of the more primitive ancestral form of the TCR signaling complex found in chickens. In contrast to mammals, chickens do not express separate CD3δ and CD3γ chains but instead encode a single hybrid chain, termed CD3δ/γ, that is capable of pairing with CD3ε. The NMR structure of the chicken CD3εδ/γ heterodimer revealed a unique dimer interface that results in a heterodimer with considerable deviation from the distinct side-by-side architecture found in human and murine CD3εδ and CD3εγ. The chicken CD3εδ/γ heterodimer also contains a unique molecular surface, with the vast majority of surface-exposed, nonconserved residues being clustered to a single face of the heterodimer. Using an in vitro biochemical assay, we demonstrate that CD3εδ/γ can assemble with both chicken TCRα and TCRβ via conserved polar transmembrane sites. Moreover, analogous to the human TCR signaling complex, the presence of two copies of CD3εδ/γ is required for ζζ assembly. These data provide insight into the evolution of this critical receptor signaling apparatus.