A functional hot spot for antigen recognition in a superagonist TCR/MHC complex

被引：191

作者：

Degano, M

Garcia, KC

Apostolopoulos, V

Rudolph, MG

Teyton, L

Wilson, IA ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA

来源：

IMMUNITY | 2000年 / 12卷 / 03期

关键词：

D O I：

10.1016/S1074-7613(00)80178-8

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

A longstanding question in T cell receptor signaling is how structurally similar ligands, with similar affinities, can have substantially different biological activity. The crystal structure of the 2C TCR complex of H-2K(b) with superagonist peptide SIYR at 2.8 Angstrom elucidates a structural basis for TCR discrimination of altered peptide ligands. The difference in antigen potency is modulated by two cavities in the TCR combining site, formed mainly by CDRs 3 alpha, 3 beta, and 1 beta, that complement centrally located peptide residues. This "functional hot spot" allows the TCR to finely discriminate amongst energetically similar interactions within different ligands for those in which the peptide appropriately stabilizes the TCR/pMHC complex and provides a new structural perspective for understanding differential signaling resulting from T cell cross-reactivity.

引用

页码：251 / 261

页数：11

共 61 条

[31] PROCHECK - A PROGRAM TO CHECK THE STEREOCHEMICAL QUALITY OF PROTEIN STRUCTURES [J].