TY - JOUR
T1 - Nonclassical binding of formylated peptide in crystal structure of MHC Class Ib molecules H2-M3
AU - Wang, Chyung Ru
AU - Castaño, A. Raúl
AU - Peterson, Per A.
AU - Slaughter, Clive
AU - Fischer Lindahl, Kirsten
AU - Deisenhofer, Johann
PY - 1995/8/25
Y1 - 1995/8/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029091980&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(95)90037-3
DO - 10.1016/0092-8674(95)90037-3
M3 - Article
C2 - 7664344
SN - 0092-8674
VL - 82
SP - 655
EP - 664
JO - Cell
JF - Cell
IS - 4
ER -