1G0X

CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)

Summary for 1G0X

• Entry DOI: 10.2210/pdb1g0x/pdb
• Descriptor: LEUCOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR-1 (2 entities in total)
• Functional Keywords: immunoglobulin fold, 3-10 helix, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: Q8NHL6
• Total number of polymer chains: 1
• Total formula weight: 21998.65

Authors

Chapman, T.L.,Heikema, A.P.,West Jr., A.P.,Bjorkman, P.J. (deposition date: 2000-10-09, release date: 2001-01-17, Last modification date: 2024-11-06)

Primary citation

Chapman, T.L.,Heikema, A.P.,West Jr., A.P.,Bjorkman, P.J.
Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2).
Immunity, 13:727-736, 2000

PubMed Abstract: 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.

PubMed: 11114384
DOI: 10.1016/S1074-7613(00)00071-6

Experimental method

X-RAY DIFFRACTION (2.1 Å)