2dyp

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spinqualitylabelsall models 2dyp, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

HLA-G is a nonclassical MHC class I (MHCI) molecule that can suppress a, wide range of immune responses in the maternal-fetal interface. The human, inhibitory immune receptors leukocyte Ig-like receptor (LILR) B1 [also, called LIR1, Ig-like transcript 2 (ILT2), or CD85j] and LILRB2, (LIR2/ILT4/CD85d) preferentially recognize HLA-G. HLA-G inherently, exhibits various forms, including beta(2)-microglobulin (beta(2)m)-free, and disulfide-linked dimer forms. Notably, LILRB1 cannot recognize the, beta(2)m-free form of HLA-G or HLA-B27, but LILRB2 can recognize the, beta(2)m-free form of HLA-B27. To date, the structural basis for, HLA-G/LILR recognition remains to be examined. Here, we report the 2.5-A, resolution crystal structure of the LILRB2/HLA-G complex. LILRB2 exhibits, an overlapping but distinct MHCI recognition mode compared with LILRB1 and, dominantly recognizes the hydrophobic site of the HLA-G alpha3 domain. NMR, binding studies also confirmed these LILR recognition differences on both, conformed (heavy chain/peptide/beta(2)m) and free forms of beta(2)m., Binding studies using beta(2)m-free MHCIs revealed differential, beta(2)m-dependent LILR-binding specificities. These results suggest that, subtle structural differences between LILRB family members cause the, distinct binding specificities to various forms of HLA-G and other MHCIs, which may in turn regulate immune suppression.

Disease

Known diseases associated with this structure: Asthma, susceptibility to OMIM:[142871], Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

2DYP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)., Shiroishi M, Kuroki K, Rasubala L, Tsumoto K, Kumagai I, Kurimoto E, Kato K, Kohda D, Maenaka K, Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16412-7. Epub 2006 Oct 20. PMID:17056715

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