2rgi: Difference between revisions
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==Crystal structure of Ca2+-free S100A2 at 1.6 A resolution== | ==Crystal structure of Ca2+-free S100A2 at 1.6 A resolution== | ||
<StructureSection load='2rgi' size='340' side='right' caption='[[2rgi]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2rgi' size='340' side='right' caption='[[2rgi]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100A2, S100L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100A2, S100L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgi OCA], [http://pdbe.org/2rgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rgi RCSB], [http://www.ebi.ac.uk/pdbsum/2rgi PDBsum]</span></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=2rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgi OCA], [http://pdbe.org/2rgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rgi RCSB], [http://www.ebi.ac.uk/pdbsum/2rgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgi_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgi_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 14:12, 5 September 2018
Crystal structure of Ca2+-free S100A2 at 1.6 A resolutionCrystal structure of Ca2+-free S100A2 at 1.6 A resolution
Structural highlights
Function[S10A2_HUMAN] May act as a modulator against excess calcium accumulation in normal human mammary epithelial cells. May also play a role in suppressing tumor cell growth.[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 PubMedS100A2 is an EF hand-containing Ca(2+)-binding protein of the family of S100 proteins. The protein is localized exclusively in the nucleus and is involved in cell cycle regulation. It attracted most interest by its function as a tumor suppressor via p53 interaction. We determined the crystal structure of homodimeric S100A2 in the Ca(2+)-free state at 1.6-A resolution. The structure revealed structural differences between subunits A and B, especially in the conformation of a loop that connects the N- and C-terminal EF hands and represents a part of the target-binding site in S100 proteins. Analysis of the hydrogen bonding network and molecular dynamics calculations indicate that one of the two observed conformations is more stable. The structure revealed Na(+) bound to each N-terminal EF hand of both subunits coordinated by oxygen atoms of the backbone carbonyl and water molecules. Comparison with the structures of Ca(2+)-free S100A3 and S100A6 suggests that Na(+) might occupy the S100-specific EF hand in the Ca(2+)-free state. Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution.,Koch M, Diez J, Fritz G J Mol Biol. 2008 May 9;378(4):933-42. Epub 2008 Mar 19. PMID:18394645[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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