Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor
Abstract
Leukocyte immunoglobulin-like receptor 1 (LIR-1), an inhibitory receptor expressed on monocytes, dendritic cells and lymphocytes, regulates cellular function by binding a broad range of classical and nonclassical major histocompatibility complex (MHC) class I molecules, and the human cytomegalovirus MHC class I homolog UL18. Here we describe the 3.4-Å crystal structure of a complex between the LIR-1 D1D2 domains and the MHC class I molecule HLA-A2. LIR-1 contacts the mostly conserved β_2-microglobulin and 3 domains of HLA-A2. The LIR-1 binding site comprises residues at the interdomain hinge, and a patch at the D1 tip. The structure shows how LIR-1 recognizes UL18 and diverse MHC class I molecules, and indicates that a similar mode of MHC class I recognition is used by other LIR family members.
Additional Information
© 2003 Nature Publishing Group. Received 22 April; accepted 9 July 2003; published online: 3 August 2003. We thank members of the Bjorkman laboratory for technical assistance, and C. O'Callaghan and A. van der Merwe for critical reading of the manuscript. B.E.W. was supported by a Wellcome Trust Travelling Fellowship and is now funded by a Medical Research Council Career Development Award. The authors declare that they have no competing financial interests. Accession numbers: Coordinates of the structure have been deposited with the Protein Data Bank under accession code 1P7Q. Protein Data Bank accession codes: LIR-1 D1D2, 1G0X; HLA-A2, 1AKJ.Attached Files
Supplemental Material - ni961-S1.pdf
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Additional details
- Eprint ID
- 75430
- DOI
- 10.1038/ni961
- Resolver ID
- CaltechAUTHORS:20170327-140338649
- Wellcome Trust
- Medical Research Council (UK)
- Created
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2017-03-27Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field