3t0h
From Proteopedia
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| - | [[ | + | ==Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90== |
| + | <StructureSection load='3t0h' size='340' side='right' caption='[[3t0h]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3t0h]] 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=3T0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0H FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t0z|3t0z]], [[3t10|3t10]], [[3t1k|3t1k]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90A, HSP90AA1, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3t0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0h RCSB], [http://www.ebi.ac.uk/pdbsum/3t0h PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein. Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90. Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity. | ||
| - | + | Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.,Li J, Sun L, Xu C, Yu F, Zhou H, Zhao Y, Zhang J, Cai J, Mao C, Tang L, Xu Y, He J Acta Biochim Biophys Sin (Shanghai). 2012 Apr;44(4):300-6. doi:, 10.1093/abbs/gms001. Epub 2012 Feb 7. PMID:22318716<ref>PMID:22318716</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Heat Shock Proteins|Heat Shock Proteins]] | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Li, J | + | [[Category: Li, J]] |
[[Category: Atpase]] | [[Category: Atpase]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
Revision as of 12:37, 9 December 2014
Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90
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Categories: Homo sapiens | Li, J | Atpase | Chaperone
