CRYSTAL-STRUCTURE OF THE HUMAN CLASS-II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA-VIRUS PEPTIDE

被引：1424

作者：

STERN, LJ

BROWN, JH

JARDETZKY, TS

GORGA, JC

URBAN, RG

STROMINGER, JL

WILEY, DC

机构：

[1] HARVARD UNIV,HOWARD HUGHES MED INST,CAMBRIDGE,MA 02138

[2] HARVARD UNIV,DEPT BIOCHEM & MOLEC BIOL,CAMBRIDGE,MA 02138

[3] BRANDEIS UNIV,ROSENSTIEL RES CTR,WALTHAM,MA 02254

[4] CHILDRENS HOSP PITTSBURGH,RANGOS RES CTR,PITTSBURGH,PA 15213

[5] UNIV PITTSBURGH,MED CTR,PITTSBURGH,PA 15213

来源：

NATURE | 1994年 / 368卷 / 6468期

关键词：

D O I：

10.1038/368215a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

引用

页码：215 / 221

页数：7

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