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Immunity. 2000 Nov;13(5):727-36.

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

Author information

1
Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, USA.

Abstract

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.

PMID:
11114384
DOI:
10.1016/s1074-7613(00)00071-6
[Indexed for MEDLINE]
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