PDBsum entry 4udt

Immune system

PDB id: 4udt

Contents

Protein chains

202 a.a.

241 a.a.

Ligands

GOL

Waters ×309

PDB id:

4udt

Name:

Immune system

Title:

T cell receptor (trav22,trbv7-9) structure

Structure:

T cell receptor alpha chain, t-cell receptor alpha chain c region. Chain: a. Fragment: variable domain trav22, residues 1-112, constant domain trac1, residues 2-95. Engineered: yes. Mutation: yes. Protein trbv7-9, t-cell receptor beta-2 chain c region. Chain: b.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell: t-lymphocyte. Gene: trac, tcra. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: star. Gene: tcrbv6s4a1, trbv7-9, trbc2, tcrbc2.

Resolution:

1.35Å R-factor: 0.158 R-free: 0.193

Authors:

K.E.J.Rodstrom,P.Regenthal,K.Lindkvist-Petersson

Key ref:

K.E.Rödström et al. (2015). Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition. Plos One, 10, e0131988. PubMed id: 26147596 DOI: 10.1371/journal.pone.0131988

Date:

11-Dec-14 Release date: 24-Jun-15

Protein chain

A0A0B4J277  (TVA22_HUMAN) -  T cell receptor alpha variable 22 from Homo sapiens

Seq: 110 a.a.

Struc: 202 a.a.*

Protein chain

P01848  (TCA_HUMAN) -  T cell receptor alpha chain constant from Homo sapiens

Seq: 140 a.a.

Struc: 202 a.a.*

Protein chain

A0A5A3  (A0A5A3_HUMAN) -  V_segment translation product (Fragment) from Homo sapiens

Seq: 116 a.a.

Struc: 241 a.a.*

Protein chain

A0A5B9  (TRBC2_HUMAN) -  T cell receptor beta constant 2 from Homo sapiens

Seq: 178 a.a.

Struc: 241 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1371/journal.pone.0131988

Plos One 10:e0131988 (2015)

PubMed id: 26147596

Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.

K.E.Rödström, P.Regenthal, K.Lindkvist-Petersson.

ABSTRACT

T cells are crucial players in cell-mediated immunity. The specificity of their receptor, the T cell receptor (TCR), is central for the immune system to distinguish foreign from host antigens. Superantigens are bacterial toxins capable of inducing a toxic immune response by cross-linking the TCR and the major histocompatibility complex (MHC) class II and circumventing the antigen specificity. Here, we present the structure of staphylococcal enterotoxin E (SEE) in complex with a human T cell receptor, as well as the unligated T cell receptor structure. There are clear structural changes in the TCR loops upon superantigen binding. In particular, the HV4 loop moves to circumvent steric clashes upon complex formation. In addition, a predicted ternary model of SEE in complex with both TCR and MHC class II displays intermolecular contacts between the TCR α-chain and the MHC, suggesting that the TCR α-chain is of importance for complex formation.