1kt2
CRYSTAL STRUCTURE OF CLASS II MHC MOLECULE IEK BOUND TO MOTH CYTOCHROME C PEPTIDE
|
OverviewOverview
The COOH-terminal peptides of pigeon and moth cytochrome c, bound to mouse, IE(k), are two of the most thoroughly studied T cell antigens. We have, solved the crystal structures of the moth peptide and a weak, agonist-antagonist variant of the pigeon peptide bound to IE(k). The moth, peptide and all other peptides whose structures have been solved bound to, IE(k), have a lysine filling the p9 pocket of IE(k). However, the pigeon, peptide has an alanine at p9 shifting the lysine to p10. Rather than, kinking to place the lysine in the anchor pocket, the pigeon peptide takes, the extended course through the binding groove, which is characteristic of, all other peptides bound to major histocompatibility complex (MHC) class, II. Thus, unlike MHC class I, in which peptides often kink to place, optimally anchoring side chains, MHC class II imposes an extended peptide, conformation even at the cost of a highly conserved anchor residue. The, substitution of Ser for Thr at p8 in the variant pigeon peptide induces no, detectable surface change other than the loss of the side chain methyl, group, despite the dramatic change in recognition by T cells. Finally, these structures can be used to interpret the many published mutational, studies of these ligands and the T cell receptors that recognize them.
About this StructureAbout this Structure
1KT2 is a Protein complex structure of sequences from Mus musculus and Moth and mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of cytochrome c presentation by IE(k)., Fremont DH, Dai S, Chiang H, Crawford F, Marrack P, Kappler J, J Exp Med. 2002 Apr 15;195(8):1043-52. PMID:11956295
Page seeded by OCA on Tue Nov 20 19:49:38 2007