Published November 1, 2000
| public
Journal Article
Crystal Structure and Ligand Binding Properties of the D1D2 Region of the Inhibitory Receptor LIR-1 (ILT2)
Chicago
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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 Å 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.
Additional Information
© 2000 Cell Press. Received 15 August 2000, Revised 11 October 2000, Available online 11 April 2001. We thank Z. Hamburger, B. Willcox, and C. O'Callaghan for assistance with crystallographic software and many helpful discussions, and D. Cosman and members of the Bjorkman lab for critical reading of the manuscript. This work was supported by a grant from the Arthritis Foundation (P. J. B.). Atomic coordinates have been deposited in the Protein Data Bank under accession code 1GOX.Additional details
- Eprint ID
- 75416
- Resolver ID
- CaltechAUTHORS:20170327-112025245
- Arthritis Foundation
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