1g0x

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{{Structure
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'''CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)'''
'''CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)'''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:59:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:13 2008''
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Revision as of 13:59, 2 May 2008

Template:STRUCTURE 1g0x

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


Overview

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.

About this Structure

1G0X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2)., Chapman TL, Heikema AP, West AP Jr, Bjorkman PJ, Immunity. 2000 Nov;13(5):727-36. PMID:11114384 Page seeded by OCA on Fri May 2 16:59:38 2008

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