2ve6

From Proteopedia

Revision as of 15:39, 4 May 2008

Template:STRUCTURE 2ve6

CRYSTAL STRUCTURE OF A MURINE MHC CLASS I H2-DB MOLECULE IN COMPLEX WITH A PHOTOCLEAVABLE PEPTIDE

Overview

Class I MHC tetramers allow direct phenotypic identification of CD8(+) T cell populations, but their production remains laborious. A peptide exchange strategy that employs class I MHC products loaded with conditional ligands (caged MHC molecules) provides a fast and straightforward method to obtain diverse arrays of class I MHC tetramers and facilitates CD8(+) T cell epitope discovery. Here, we describe the development of photocleavable analogs of the FAPGNYPAL (SV9) epitope that bind H-2K(b) and H-2D(b) with full retention of their structural and functional integrity. We ranked all possible H-2K(b) octameric and H-2D(b) nonameric epitopes that span the genome of Chlamydia trachomatis and prepared MHC tetramers from approximately 2,000 of the highest scoring peptides by replacement of the SV9 analog with the peptide of choice. The resulting 2,000-member class I MHC tetramer array allowed the discovery of two variants of an epitope derived from polymorphic membrane protein I (PmpI) and an assessment of the kinetics of emergence and the effector function of the corresponding CD8(+) T cells.

About this Structure

2VE6 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Discovery of CD8+ T cell epitopes in Chlamydia trachomatis infection through use of caged class I MHC tetramers., Grotenbreg GM, Roan NR, Guillen E, Meijers R, Wang JH, Bell GW, Starnbach MN, Ploegh HL, Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3831-6. Epub 2008 Feb 1. PMID:18245382 Page seeded by OCA on Sun May 4 18:39:16 2008