Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor.

Willcox BE; Thomas LM; Bjorkman PJ

doi:10.1038/ni961

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-A 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 beta(2)-microglobulin and alpha3 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.

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Data

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This data has been provided by curated databases and other sources that have cited the article.

Proteins in UniProt (4)

Gag-Pol polyprotein(UniProt - P12499)
Leukocyte immunoglobulin-like receptor subfamily B member 1(UniProt - Q8NHL6)
HLA class I histocompatibility antigen, A alpha chain(UniProt - P04439)
Beta-2-microglobulin(UniProt - P61769)

Protein interactions in IntAct

b2m-gag_pol-1(IntAct - EBI-14032852)

Protein structures in PDBe

crystal structure of hla-a2 bound to lir-1, a host and viral mhc receptor(PDB - 1p7q)
View structure

Protocols & materials

Related Immune Epitope Information - Immune Epitope Database and Analysis Resource

http://www.iedb.org/pmId/12897781

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