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Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides.

Abstract：

:Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ciatto C,Tissot AC,Tschopp M,Capitani G,Pecorari F,Plückthun A,Grütter MG

doi

10.1006/jmbi.2001.5016

keywords:

subject

Has Abstract

pub_date

2001-10-05 00:00:00

pages

1059-71

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(01)95016-8

journal_volume

312

pub_type

杂志文章

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