2GW5

Crystal Structure of LIR-2 (ILT4) at 1.8 : differences from LIR-1 (ILT2) in regions implicated in the binding of the Cytomegalovirus class I MHC homolog UL18

Summary for 2GW5

• Entry DOI: 10.2210/pdb2gw5/pdb
• Descriptor: Leukocyte immunoglobulin-like receptor subfamily B member 2 precursor, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: ig like domains, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: Q8N423
• Total number of polymer chains: 1
• Total formula weight: 21994.79

Authors

Willcox, B.E.,Thomas, L.M.,Chapman, T.L.,Heikema, A.P.,West, A.P.,Bjorkman, P.J. (deposition date: 2006-05-03, release date: 2006-06-20, Last modification date: 2024-10-16)

Primary citation

Willcox, B.E.,Thomas, L.M.,Chapman, T.L.,Heikema, A.P.,West, A.P.,Bjorkman, P.J.
Crystal structure of LIR-2 (ILT4) at 1.8 A: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18.
Bmc Struct.Biol., 2:6-6, 2002

PubMed Abstract: Leukocyte Immunoglobulin-like Receptor-1 (LIR-1) and LIR-2 (also known as ILT2 and ILT4 respectively) are highly related cell surface receptors that bind a broad range of class I MHC molecules with low (microM) affinities. Expressed on monocytic cells and macrophages, both molecules transmit inhibitory signals after binding ligands. In addition to binding host class I MHC, the LIR-1 molecule, which is also expressed on lymphoid tissues, binds with a high (nM) affinity to UL18, a class I MHC homolog encoded by Human Cytomegalovirus (HCMV). In comparison, LIR-2 binds UL18 only weakly (microM KD). To understand how HCMV preferentially targets the more broadly expressed LIR-1 molecule, we determined the crystal structure of a ligand-binding fragment of LIR-2, and compared this to the existing high-resolution crystal structure of LIR-1.

PubMed: 12390682
DOI: 10.1186/1472-6807-2-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)