1sjh
From Proteopedia
| |||||||
| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | HLA-DRA (Homo sapiens), HLA-DRB1 (Homo sapiens), ENTC3, SAV2009, SA1817 (Staphylococcus aureus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HLA-DR1 complexed with a 13 residue HIV capsid peptide
Overview
T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction.
About this Structure
1SJH is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition., Zavala-Ruiz Z, Strug I, Walker BD, Norris PJ, Stern LJ, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13279-84. Epub 2004 Aug 26. PMID:15331779
Page seeded by OCA on Thu Mar 20 14:05:45 2008
