1MHC

MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION

Summary for 1MHC

• Entry DOI: 10.2210/pdb1mhc/pdb
• Descriptor: MHC CLASS I ANTIGEN H2-M3, NONAPEPTIDE FROM RAT NADH DEHYDROGENASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: histocompatibility antigen/peptide, histocompatibility antigen-peptide complex
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 6
• Total formula weight: 91242.04

Authors

Wang, C.-R.,Fischer Lindahl, K.,Deisenhofer, J. (deposition date: 1995-08-23, release date: 1996-01-29, Last modification date: 2024-11-20)

Primary citation

Wang, C.R.,Castano, A.R.,Peterson, P.A.,Slaughter, C.,Lindahl, K.F.,Deisenhofer, J.
Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3
Cell(Cambridge,Mass.), 82:655-664, 1995

PubMed 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.

PubMed: 7664344
DOI: 10.1016/0092-8674(95)90037-3

Experimental method

X-RAY DIFFRACTION (2.1 Å)