Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2)

被引：120

作者：

Chapman, TL

Heikema, AP

West, AP

Bjorkman, PJ ^{[1
]}

机构：

[1] CALTECH, Div Biol, Pasadena, CA 91125 USA

[2] CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA

来源：

IMMUNITY | 2000年 / 13卷 / 05期

关键词：

D O I：

10.1016/S1074-7613(00)00071-6

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

LIR-1 is an inhibitory receptor that recognizes class I MHC molecules and the human cytomegalovirus class I homolog UL18. Here, we report the 2.1 A resolution crystal structure of the ligand binding portion of LIR-1 (domains 1 and 2 [D1D2]) and localize the binding region for UL18. LIR-1 D1D2 is composed of two immunoglobulin-like domains arranged at an acute angle to form a bent structure resembling the structures of natural killer inhibitory receptors (KIRs). The LIR-1 binding site comprises a portion of D1 distant from the interdomain hinge region that constitutes the KIR binding site, consistent with differences in LIR-1 and KIR recognition properties and functions.

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页码：727 / 736

页数：10

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