2nms

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(New page: 200px<br /> <applet load="2nms" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nms, resolution 2.60&Aring;" /> '''The Crystal Structu...)
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[[Image:2nms.gif|left|200px]]<br />
 
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<applet load="2nms" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2nms, resolution 2.60&Aring;" />
 
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'''The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1'''<br />
 
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==Overview==
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==The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1==
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The immune receptors expressed on myeloid cells (IREM) are type I, transmembrane proteins encoded on human chromosome 17 (17q25.1), whose, function is believed to be important in controlling inflammation. To date, three IREM receptors have been identified. IREM-1 functions as an, inhibitory receptor, whereas IREM-2 and IREM-3 serve an activating, function. Here, we report the crystal structure of IREM-1 extracellular, domain at 2.6 A resolution. The overall fold of IREM-1 resembles that of a, V-type immunoglobulin domain, and reveals overall close homology with, immunoglobulin domains from other immunoreceptors such as CLM-1, TREM-1, TLT-1 and NKp44. Comparing the surface electrostatic potential and, hydrophobicity of IREM-1 with its murine homologous CLM-1, we observed, unique structural properties for the complementary determining region of, IREM-1, which suggests that they may be involved in recognition of the, IREM-1 ligand. Particularly interesting is the structural conformation and, physical properties of the antibody's equivalent CDR3 loop, which we show, to be a structurally variable region of the molecule and therefore could, be the main structural determinant for ligand discrimination and binding., In addition, the analysis of the IREM-1 structure revealed the presence of, four structurally different cavities. Three of these cavities form a, continuous hydrophobic groove on the IREM-1 surface, which point to a, region of the molecule capable of accommodating potential ligands.
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<StructureSection load='2nms' size='340' side='right'caption='[[2nms]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2nms]] 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=2NMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NMS 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]] 2.6&#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=2nms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nms OCA], [https://pdbe.org/2nms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nms RCSB], [https://www.ebi.ac.uk/pdbsum/2nms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nms ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLM1_HUMAN CLM1_HUMAN] Acts as an inhibitory receptor for myeloid cells and mast cells. Inhibits osteoclast formation.<ref>PMID:15549731</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/nm/2nms_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=2nms 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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The immune receptors expressed on myeloid cells (IREM) are type I transmembrane proteins encoded on human chromosome 17 (17q25.1), whose function is believed to be important in controlling inflammation. To date, three IREM receptors have been identified. IREM-1 functions as an inhibitory receptor, whereas IREM-2 and IREM-3 serve an activating function. Here, we report the crystal structure of IREM-1 extracellular domain at 2.6 A resolution. The overall fold of IREM-1 resembles that of a V-type immunoglobulin domain, and reveals overall close homology with immunoglobulin domains from other immunoreceptors such as CLM-1, TREM-1, TLT-1 and NKp44. Comparing the surface electrostatic potential and hydrophobicity of IREM-1 with its murine homologous CLM-1, we observed unique structural properties for the complementary determining region of IREM-1, which suggests that they may be involved in recognition of the IREM-1 ligand. Particularly interesting is the structural conformation and physical properties of the antibody's equivalent CDR3 loop, which we show to be a structurally variable region of the molecule and therefore could be the main structural determinant for ligand discrimination and binding. In addition, the analysis of the IREM-1 structure revealed the presence of four structurally different cavities. Three of these cavities form a continuous hydrophobic groove on the IREM-1 surface, which point to a region of the molecule capable of accommodating potential ligands.
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==About this Structure==
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The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1.,Marquez JA, Galfre E, Dupeux F, Flot D, Moran O, Dimasi N J Mol Biol. 2007 Mar 23;367(2):310-8. Epub 2007 Jan 10. PMID:17275839<ref>PMID:17275839</ref>
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2NMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2NMS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1., Marquez JA, Galfre E, Dupeux F, Flot D, Moran O, Dimasi N, J Mol Biol. 2007 Mar 23;367(2):310-8. Epub 2007 Jan 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17275839 17275839]
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</div>
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<div class="pdbe-citations 2nms" style="background-color:#fffaf0;"></div>
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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: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dimasi, N.]]
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[[Category: Dimasi N]]
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[[Category: Marquez, J.A.]]
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[[Category: Marquez JA]]
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[[Category: ig-superfamily]]
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[[Category: ig-v]]
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[[Category: inhibitory receptor]]
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[[Category: membrane protein]]
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[[Category: myelo-monocytic cells]]
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[[Category: myeloid ig-like receptor]]
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[[Category: negative regulation of leukocyte]]
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[[Category: nkp44-like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:59:38 2007''
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Current revision

The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1

PDB ID 2nms

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