Nonclassical binding of formylated peptide in crystal structure of the MHC class lb molecule H2-M3

H2-M3 is a class Ib MHC molecule of the mouse with a 10 4-fold preference for binding N-fonmylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a fonnylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray cry...

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Bibliographic Details
Published in:Cell 1995-08, Vol.82 (4), p.655-664
Main Authors: Wang, Chyung-Ru, Castan˜o, A. Rau´l, Peterson, Per A., Slaughter, Clive, Fischer Lindahl, Kirsten, Deisenhofer, Johann
Format: Article
Language:English
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Summary:H2-M3 is a class Ib MHC molecule of the mouse with a 10 4-fold preference for binding N-fonmylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a fonnylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1A˚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.
ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(95)90037-3