2cii

From Proteopedia

Revision as of 17:14, 18 December 2007

THE CRYSTAL STRUCTURE OF H-2DB COMPLEXED WITH A PARTIAL PEPTIDE EPITOPE SUGGESTS AN MHC CLASS I ASSEMBLY-INTERMEDIATE

Overview

In the absence of bound peptide ligands, major histocompatibility complex, (MHC) class I molecules are unstable. In an attempt to determine the, minimum requirement for peptide-dependent MHC class I stabilization, we, have used short synthetic peptides derived from the Sendai virus, nucleoprotein epitope (residues 324-332, 1FAPGNYPAL9) to promote its, folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by, the pentapeptide 5NYPAL9, which is equivalent to the C-terminal portion of, the optimal nonapeptide and includes both the P5 and P9 anchor residues., We have crystallized the complex of the H-2D(b) molecule with the pentamer, and determined the structure to show how a quasi-stable MHC class I, molecule can be formed by occupancy of a single binding pocket in the, peptide-binding groove.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

2CII is a Protein complex structure of sequences from Homo sapiens and Mus musculus with GOL as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate., Glithero A, Tormo J, Doering K, Kojima M, Jones EY, Elliott T, J Biol Chem. 2006 May 5;281(18):12699-704. Epub 2006 Feb 14. PMID:16478731

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