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2nms

From Proteopedia

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

Structural highlights

2nms is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLM1_HUMAN Acts as an inhibitory receptor for myeloid cells and mast cells. Inhibits osteoclast formation.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Alvarez-Errico D, Aguilar H, Kitzig F, Brckalo T, Sayos J, Lopez-Botet M. IREM-1 is a novel inhibitory receptor expressed by myeloid cells. Eur J Immunol. 2004 Dec;34(12):3690-701. PMID:15549731 doi:http://dx.doi.org/10.1002/eji.200425433
↑ Marquez JA, Galfre E, Dupeux F, Flot D, Moran O, Dimasi N. The crystal structure of the extracellular domain of the inhibitor receptor expressed on myeloid cells IREM-1. J Mol Biol. 2007 Mar 23;367(2):310-8. Epub 2007 Jan 10. PMID:17275839 doi:10.1016/j.jmb.2007.01.011

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nms"

Categories: Homo sapiens | Large Structures | Dimasi N | Marquez JA

@@ Line 1: / Line 1: @@
 ==The Crystal Structure of the Extracellular Domain of the Inhibitor Receptor Expressed on Myeloid Cells IREM-1==
-<StructureSection load='2nms' size='340' side='right' caption='[[2nms]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='2nms' size='340' side='right'caption='[[2nms]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nms]] is a 1 chain structure with 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=2NMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NMS FirstGlance]. <br>
+<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>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD300LF, CLM1, IGSF13, IREM1, NKIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nms OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nms RCSB], [http://www.ebi.ac.uk/pdbsum/2nms PDBsum]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[http://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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/2nms_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/2nms_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2nms" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Dimasi, N]]
+[[Category: Large Structures]]
-[[Category: Marquez, J A]]
+[[Category: Dimasi N]]
-[[Category: Ig-superfamily]]
+[[Category: Marquez JA]]
-[[Category: Ig-v]]
-[[Category: Immune system]]
-[[Category: Inhibitory receptor]]
-[[Category: Membrane protein]]
-[[Category: Myelo-monocytic cell]]
-[[Category: Myeloid ig-like receptor]]
-[[Category: Negative regulation of leukocyte]]
-[[Category: Nkp44-like]]

2nms

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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