2d3v

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[[Image:2d3v.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)==
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|PDB= 2d3v |SIZE=350|CAPTION= <scene name='initialview01'>2d3v</scene>, resolution 1.85&Aring;
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<StructureSection load='2d3v' size='340' side='right'caption='[[2d3v]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[2d3v]] is a 1 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=2D3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3V FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.85&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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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=2d3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3v OCA], [https://pdbe.org/2d3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3v RCSB], [https://www.ebi.ac.uk/pdbsum/2d3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3v ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3v OCA], [http://www.ebi.ac.uk/pdbsum/2d3v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d3v RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LIRA5_HUMAN LIRA5_HUMAN] May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition.<ref>PMID:16675463</ref>
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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/d3/2d3v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2d3v 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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Human leukocyte Ig-like receptor B1 (LILRB1) and B2 (LILRB2) belong to "Group 1" receptors and recognize a broad range of major histocompatibility complex class I molecules (MHCIs). In contrast, "Group 2" receptors show low similarity with LILRB1/B2, and their ligands remain to be identified. To date, the structural and functional characteristics of Group 2 LILRs are poorly understood. Here we report the crystal structure of the extracellular domain of LILRA5, which is an activating Group 2 LILR expressed on monocytes and neutrophils. Unexpectedly, the structure showed large changes in structural conformation and charge distribution in the region corresponding to the MHCI binding site of LILRB1/B2, which are also distinct from killer cell Ig-like receptors and Fc alpha receptors. These changes probably confer the structural hindrance for the MHCI binding, and their key amino acid substitutions are well conserved in Group 2 LILRs. Consistently, the surface plasmon resonance and flow cytometric analyses demonstrated that LILRA5 exhibited no affinities to all tested MHCIs. These results raised the possibility that LILRA5 as well as Group 2 LILRs do not play a role in any MHCI recognition but could possibly bind to non-MHCI ligand(s) on the target cells to provide a novel immune regulation mechanism.
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'''Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)'''
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Crystal structure of the human monocyte-activating receptor, "Group 2" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11).,Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K J Biol Chem. 2006 Jul 14;281(28):19536-44. Epub 2006 May 3. PMID:16675463<ref>PMID:16675463</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2d3v" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Human leukocyte Ig-like receptor B1 (LILRB1) and B2 (LILRB2) belong to "Group 1" receptors and recognize a broad range of major histocompatibility complex class I molecules (MHCIs). In contrast, "Group 2" receptors show low similarity with LILRB1/B2, and their ligands remain to be identified. To date, the structural and functional characteristics of Group 2 LILRs are poorly understood. Here we report the crystal structure of the extracellular domain of LILRA5, which is an activating Group 2 LILR expressed on monocytes and neutrophils. Unexpectedly, the structure showed large changes in structural conformation and charge distribution in the region corresponding to the MHCI binding site of LILRB1/B2, which are also distinct from killer cell Ig-like receptors and Fc alpha receptors. These changes probably confer the structural hindrance for the MHCI binding, and their key amino acid substitutions are well conserved in Group 2 LILRs. Consistently, the surface plasmon resonance and flow cytometric analyses demonstrated that LILRA5 exhibited no affinities to all tested MHCIs. These results raised the possibility that LILRA5 as well as Group 2 LILRs do not play a role in any MHCI recognition but could possibly bind to non-MHCI ligand(s) on the target cells to provide a novel immune regulation mechanism.
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*[[Leukocyte immunoglobulin-like receptor|Leukocyte immunoglobulin-like receptor]]
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== References ==
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==About this Structure==
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<references/>
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2D3V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3V OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of the human monocyte-activating receptor, "Group 2" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11)., Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K, J Biol Chem. 2006 Jul 14;281(28):19536-44. Epub 2006 May 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16675463 16675463]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kajikawa, M.]]
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[[Category: Kajikawa M]]
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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: Ose, T.]]
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[[Category: Ose T]]
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[[Category: Shiroishi, M.]]
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[[Category: Shiroishi M]]
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[[Category: immunoglobulin-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:58 2008''
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Current revision

Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)

PDB ID 2d3v

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