Nonclassical binding of formylated peptide in crystal structure of MHC Class Ib molecules H2-M3

Chyung Ru Wang*, A. Raúl Castaño, Per A. Peterson, Clive Slaughter, Kirsten Fischer Lindahl, Johann Deisenhofer

*Autor corresponent d’aquest treball

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Resum

H2-M3 is a class Ib MHC molecule of the mouse with a 104-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 2.1 Å 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.

Idioma originalEnglish
Pàgines (de-a)655-664
Nombre de pàgines10
RevistaCell
Volum82
Número4
DOIs
Estat de la publicacióPublicada - 25 d’ag. 1995

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