1P7Q

Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor

Summary for 1P7Q

• Entry DOI: 10.2210/pdb1p7q/pdb
• Descriptor: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, POL polyprotein, ... (4 entities in total)
• Functional Keywords: hla-a2-lir-1 complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892 Q8NHL6; Secreted: P61769; Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12499
• Total number of polymer chains: 4
• Total formula weight: 66691.32

Authors

Willcox, B.E.,Thomas, L.M.,Bjorkman, P.J. (deposition date: 2003-05-05, release date: 2003-10-14, Last modification date: 2024-10-30)

Primary citation

Willcox, B.E.,Thomas, L.M.,Bjorkman, P.J.
Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor.
Nat.Immunol., 4:913-919, 2003

PubMed 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.

PubMed: 12897781
DOI: 10.1038/ni961

Experimental method

X-RAY DIFFRACTION (3.4 Å)