3t0h: Difference between revisions
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<StructureSection load='3t0h' size='340' side='right'caption='[[3t0h]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='3t0h' size='340' side='right'caption='[[3t0h]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3t0h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</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=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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li | [[Category: Li J]] | ||
Latest revision as of 20:28, 1 November 2023
Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90
Structural highlights
FunctionHS90A_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.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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