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| | ==The Structure of Ca2+-loaded S100A2 at 1.3A resolution== | | ==The Structure of Ca2+-loaded S100A2 at 1.3A resolution== |
| - | <StructureSection load='4duq' size='340' side='right' caption='[[4duq]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4duq' size='340' side='right'caption='[[4duq]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4duq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3n22 3n22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DUQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4duq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3n22 3n22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DUQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 1.3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4duq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4duq OCA], [http://pdbe.org/4duq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4duq RCSB], [http://www.ebi.ac.uk/pdbsum/4duq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4duq ProSAT]</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=4duq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4duq OCA], [https://pdbe.org/4duq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4duq RCSB], [https://www.ebi.ac.uk/pdbsum/4duq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4duq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/S10A2_HUMAN 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.<ref>PMID:1372446</ref> | + | [https://www.uniprot.org/uniprot/S10A2_HUMAN 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.<ref>PMID:1372446</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | S100A2 is an EF-hand Ca(2+) -binding protein that activates the tumor suppressor p53. In order to understand the molecular mechanisms underlying the Ca(2+) -induced activation of S100A2 the structure of Ca(2+) -bound S100A2 was determined at 1.3 A resolution by X-ray crystallography. The structure was compared to Ca(2+) -free S100A2 and to other S100 proteins. Ca(2+) binding to S100A2 induces small structural changes in the N-terminal EF-hand, but a large conformational change in the C-terminal EF-hand reorienting helix III by approximately 90 degrees is observed. This movement is accompanied by the exposure of a hydrophobic cavity between helix III and helix IV that represents the target protein interaction site. This molecular reorganization is associated with the breaking and new formation of intramolecular hydrophobic contacts. The target binding site exhibits unique features; in particular the hydrophobic cavity is larger than in other Ca(2+) -loaded S100 proteins. The structural data underline that the shape and size of the hydrophobic cavity are major determinants for target specificity of S100 proteins and suggests that the binding mode for S100A2 is different from other p53-interacting S100 proteins. STRUCTURED DIGITAL ABSTRACT: S100A2 and S100A2bind by x-ray crystallography (View interaction).
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| - | The Structure of Ca(2+) -loaded S100A2 at 1.3 A resolution.,Koch M, Fritz G FEBS J. 2012 Mar 6. doi: 10.1111/j.1742-4658.2012.08556.x. PMID:22394450<ref>PMID:22394450</ref>
| + | ==See Also== |
| - | | + | *[[S100 proteins 3D structures|S100 proteins 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4duq" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Fritz, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Koch, M]] | + | [[Category: Fritz G]] |
| - | [[Category: Calcium-binding]] | + | [[Category: Koch M]] |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Metal binding protein]]
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| - | [[Category: Tumor supressor]]
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| - | [[Category: Zinc-binding]]
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