Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2)

Immunity. 2000 Nov;13(5):727-36. doi: 10.1016/s1074-7613(00)00071-6.


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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD*
  • Glycoproteins / chemistry
  • Glycoproteins / genetics
  • Glycoproteins / metabolism
  • Humans
  • Leukocyte Immunoglobulin-like Receptor B1
  • Ligands
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Receptors, Immunologic* / chemistry
  • Receptors, Immunologic* / genetics
  • Receptors, Immunologic* / metabolism
  • Receptors, Virus / chemistry
  • Receptors, Virus / genetics
  • Receptors, Virus / metabolism
  • Sequence Alignment


  • Antigens, CD
  • Glycoproteins
  • LILRB1 protein, human
  • Leukocyte Immunoglobulin-like Receptor B1
  • Ligands
  • Receptors, Immunologic
  • Receptors, Virus

Associated data

  • PDB/1GOX