2d2z: Difference between revisions

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 <StructureSection load='2d2z' size='340' side='right'caption='[[2d2z]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d2z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d2z]] is a 3 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=2D2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2Z FirstGlance]. <br>
-</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=2d2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2z OCA], [https://pdbe.org/2d2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d2z RCSB], [https://www.ebi.ac.uk/pdbsum/2d2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d2z ProSAT]</span></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]] 2.2&#8491;</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=2d2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2z OCA], [https://pdbe.org/2d2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d2z RCSB], [https://www.ebi.ac.uk/pdbsum/2d2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d2z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CLIC4_HUMAN CLIC4_HUMAN]] Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).<ref>PMID:12163372</ref> <ref>PMID:14569596</ref> <ref>PMID:16239224</ref> <ref>PMID:18302930</ref> <ref>PMID:19247789</ref> <ref>PMID:16176272</ref>
+[https://www.uniprot.org/uniprot/CLIC4_HUMAN CLIC4_HUMAN] Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).<ref>PMID:12163372</ref> <ref>PMID:14569596</ref> <ref>PMID:16239224</ref> <ref>PMID:18302930</ref> <ref>PMID:19247789</ref> <ref>PMID:16176272</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=2d2z ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of a wild type of the human soluble chloride intracellular ion channel CLIC4 (wCLIC4) has been determined at a resolution of 2.2A. The structure shows a homotrimer in an asymmetric unit, which is first observed in CLICs. The assembly of the trimer takes a unique triple interaction mode between three monomers with a hydrogen-bond network and hydrophobic contacts. Through such complicated interactions, the homotrimer of wCLIC4 is firmly stabilized. The structure shows an oligomeric mode with a unique assembly mechanism by which the oligomerization of CLIC4 can be performed without any intramolecular disulfide bond formation. It indicated a possibility that CLIC4 may take a unique structural organization distinct from CLIC1 for docking with lipid bilayers. In addition, the structure shows distinct conformational states of the h2 region for respective monomers of the trimer, which reveal an intrinsic conformational susceptibility for this significant region in the structural transition.
-Trimeric structure of the wild soluble chloride intracellular ion channel CLIC4 observed in crystals.,Li Y, Li D, Zeng Z, Wang D Biochem Biophys Res Commun. 2006 May 19;343(4):1272-8. Epub 2006 Mar 27. PMID:16581025<ref>PMID:16581025</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2d2z" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Li, D F]]
+[[Category: Li DF]]
-[[Category: Li, Y F]]
+[[Category: Li YF]]
-[[Category: Wang, D C]]
+[[Category: Wang DC]]
-[[Category: Clic4]]
-[[Category: Soluble form]]
-[[Category: Transport protein]]