3t0h

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[[Image:3t0h.jpg|left|200px]]
 
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==Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90==
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The line below this paragraph, containing "STRUCTURE_3t0h", creates the "Structure Box" on the page.
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<StructureSection load='3t0h' size='340' side='right'caption='[[3t0h]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3t0h]] 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=3T0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0H FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0h OCA], [https://pdbe.org/3t0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0h RCSB], [https://www.ebi.ac.uk/pdbsum/3t0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0h ProSAT]</span></td></tr>
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{{STRUCTURE_3t0h| PDB=3t0h | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t0h" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[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].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Li, J.]]
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[[Category: Large Structures]]
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[[Category: Atpase]]
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[[Category: Li J]]
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[[Category: Chaperone]]
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Current revision

Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90

PDB ID 3t0h

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