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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
44
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pubmed:dateCreated |
2006-11-1
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-10190906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-10227970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-10591185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-11114384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-11698424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-11839562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-11875462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12154202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12390682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12454284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12853576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12874224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12897781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-12974794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15011960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15146181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15265899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15304001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15718280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15771571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-15857883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-16014635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-16210588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-16305801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-16455647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-16675463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-2446316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-9151699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-9531263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-9548455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17056715-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/HLA Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-G Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/LILRB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/LILRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16412-7
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17056715-Antigens, CD,
pubmed-meshheading:17056715-HLA Antigens,
pubmed-meshheading:17056715-HLA-A2 Antigen,
pubmed-meshheading:17056715-HLA-G Antigens,
pubmed-meshheading:17056715-Histocompatibility Antigens Class I,
pubmed-meshheading:17056715-Humans,
pubmed-meshheading:17056715-Membrane Glycoproteins,
pubmed-meshheading:17056715-Models, Molecular,
pubmed-meshheading:17056715-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17056715-Protein Binding,
pubmed-meshheading:17056715-Protein Structure, Quaternary,
pubmed-meshheading:17056715-Protein Structure, Tertiary,
pubmed-meshheading:17056715-Receptors, Immunologic,
pubmed-meshheading:17056715-Structural Homology, Protein,
pubmed-meshheading:17056715-Surface Plasmon Resonance,
pubmed-meshheading:17056715-beta 2-Microglobulin
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pubmed:year |
2006
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pubmed:articleTitle |
Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d).
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pubmed:affiliation |
Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
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pubmed:publicationType |
Journal Article
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