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2dyp

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(New page: 200px<br /> <applet load="2dyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dyp, resolution 2.5&Aring;" /> '''Crystal Structure of...)
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[[Image:2dyp.gif|left|200px]]<br />
 
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<applet load="2dyp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2dyp, resolution 2.5&Aring;" />
 
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'''Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G'''<br />
 
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==Overview==
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==Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G==
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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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<StructureSection load='2dyp' size='340' side='right'caption='[[2dyp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2dyp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DYP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyp OCA], [https://pdbe.org/2dyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dyp RCSB], [https://www.ebi.ac.uk/pdbsum/2dyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dyp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HLAG_HUMAN HLAG_HUMAN] Involved in the presentation of foreign antigens to the immune system. Plays a role in maternal tolerance of the fetus by mediating protection from the deleterious effects of natural killer cells, cytotoxic T-lymphocytes, macrophages and mononuclear cells.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/2dyp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dyp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==Disease==
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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<ref>PMID:17056715</ref>
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Known diseases associated with this structure: Asthma, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142871 142871]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2DYP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DYP OCA].
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</div>
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<div class="pdbe-citations 2dyp" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17056715 17056715]
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[Leukocyte immunoglobulin-like receptor|Leukocyte immunoglobulin-like receptor]]
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*[[MHC 3D structures|MHC 3D structures]]
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*[[MHC I 3D structures|MHC I 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Kohda, D.]]
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[[Category: Kohda D]]
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[[Category: Kuroki, K.]]
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[[Category: Kuroki K]]
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[[Category: Maenaka, K.]]
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[[Category: Maenaka K]]
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[[Category: Rasubala, L.]]
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[[Category: Rasubala L]]
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[[Category: Shiroishi, M.]]
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[[Category: Shiroishi M]]
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[[Category: immunoglobulin-like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:41:01 2007''
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Current revision

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

PDB ID 2dyp

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