Epitopes described in "Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3."

Reference
Article Authors:C R Wang; A R CastaƱo; P A Peterson; C Slaughter; K F Lindahl; J Deisenhofer
Article Title:Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3.
Reference Detail
Reference ID:1013618
Abstract:H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference for binding N-formylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a formylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove.
Affiliations:Department of Biochemistry, University of Texas Southwestern Medical Center Dallas 75235-9050, USA.
Date:1995
Reference Type:Literature
PubMed ID:7664344
Journal:Cell
Journal Volume:82
Article Pages:655-64
Journal ISSN:0092-8674
Article Chemical List:DNA, Complementary;Histocompatibility Antigens Class I;Oligopeptides;N-Formylmethionine
Article MeSH List:Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA, Complementary(genetics); Electrochemistry; Histocompatibility Antigens Class I(chemistry; genetics; metabolism); Mice; Models, Molecular; Molecular Sequence Data; Molecular Structure; N-Formylmethionine(metabolism); Oligopeptides(chemistry; genetics; metabolism); Protein Binding; Protein Conformation
Curation Last Updated:2014-10-03 21:19:59