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

Nat Immunol. 2003 Sep;4(9):913-9. doi: 10.1038/ni961. Epub 2003 Aug 3.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • HLA-A2 Antigen / chemistry*
  • Humans
  • Leukocyte Immunoglobulin-like Receptor B1
  • Models, Molecular
  • Molecular Sequence Data
  • Receptors, Immunologic / chemistry*
  • Sequence Alignment


  • Antigens, CD
  • HLA-A2 Antigen
  • LILRB1 protein, human
  • Leukocyte Immunoglobulin-like Receptor B1
  • Receptors, Immunologic

Associated data

  • PDB/1AKJ
  • PDB/1G0X
  • PDB/1P7Q
  • PDB/D1D2