PDBsum entry 3tid

Immune system

PDB id: 3tid

Contents

Protein chains

277 a.a.

99 a.a.

Ligands

ALA-VAL-TYR-ASN-PHE-ALA-THR-MET

ACT ×3

Waters ×544

PDB id:

3tid

Name:

Immune system

Title:

Crystal structure of the lcmv derived peptide gp34 in complex with the murine mhc class i h-2 kb

Structure:

H-2 class i histocompatibility antigen, k-b alpha chain. Chain: a. Fragment: unp residues 22-297. Synonym: h-2k(b). Engineered: yes. Beta-2-microglobulin. Chain: b. Fragment: unp residues 21-119. Synonym: beta-2-microglobulin form pi 5.3.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-k1, h2-k. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

1.65Å R-factor: 0.176 R-free: 0.192

Authors:

T.T.Nguyen,Z.T.Shen,L.J.Stern

Key ref:

Z.T.Shen et al. (2013). Disparate epitopes mediating protective heterologous immunity to unrelated viruses share peptide-MHC structural features recognized by cross-reactive T cells. J Immunol, 191, 5139-5152. PubMed id: 24127554 DOI: 10.4049/jimmunol.1300852

Date:

20-Aug-11 Release date: 22-Aug-12

Protein chain

P01901  (HA1B_MOUSE) -  H-2 class I histocompatibility antigen, K-B alpha chain from Mus musculus

Seq: 369 a.a.

Struc: 277 a.a.*

Protein chain

P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens

Seq: 119 a.a.

Struc: 99 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.4049/jimmunol.1300852

J Immunol 191:5139-5152 (2013)

PubMed id: 24127554

Disparate epitopes mediating protective heterologous immunity to unrelated viruses share peptide-MHC structural features recognized by cross-reactive T cells.

Z.T.Shen, T.T.Nguyen, K.A.Daniels, R.M.Welsh, L.J.Stern.

ABSTRACT

Closely related peptide epitopes can be recognized by the same T cells and contribute to the immune response against pathogens encoding those epitopes, but sometimes cross-reactive epitopes share little homology. The degree of structural homology required for such disparate ligands to be recognized by cross-reactive TCRs remains unclear. In this study, we examined the mechanistic basis for cross-reactive T cell responses between epitopes from unrelated and pathogenic viruses, lymphocytic choriomeningitis virus (LCMV) and vaccinia virus. Our results show that the LCMV cross-reactive T cell response toward vaccinia virus is dominated by a shared asparagine residue, together with other shared structural elements conserved in the crystal structures of K(b)-VV-A11R and K(b)-LCMV-gp34. Based on analysis of the crystal structures and the specificity determinants for the cross-reactive T cell response, we were able to manipulate the degree of cross-reactivity of the T cell response, and to predict and generate a LCMV cross-reactive response toward a variant of a null OVA-derived peptide. These results indicate that protective heterologous immune responses can occur for disparate epitopes from unrelated viruses.