1MHC
MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION
1MHC の概要
エントリーDOI | 10.2210/pdb1mhc/pdb |
分子名称 | MHC CLASS I ANTIGEN H2-M3, NONAPEPTIDE FROM RAT NADH DEHYDROGENASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
機能のキーワード | histocompatibility antigen/peptide, histocompatibility antigen-peptide complex |
由来する生物種 | Mus musculus (house mouse) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 91242.04 |
構造登録者 | Wang, C.-R.,Fischer Lindahl, K.,Deisenhofer, J. (登録日: 1995-08-23, 公開日: 1996-01-29, 最終更新日: 2024-11-20) |
主引用文献 | 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 Cited by 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: 7664344DOI: 10.1016/0092-8674(95)90037-3 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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