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{{STRUCTURE_3o0i|  PDB=3o0i  |  SCENE=  }}
===Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor PU-H54===
{{ABSTRACT_PUBMED_23995768}}


==About this Structure==
==Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor PU-H54==
[[3o0i]] 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=3O0I OCA].  
<StructureSection load='3o0i' size='340' side='right'caption='[[3o0i]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3o0i]] 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=3O0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O0I FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P54:8-[(2,4-DIMETHYLPHENYL)SULFANYL]-3-PENT-4-YN-1-YL-3H-PURIN-6-AMINE'>P54</scene></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=3o0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0i OCA], [https://pdbe.org/3o0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o0i RCSB], [https://www.ebi.ac.uk/pdbsum/3o0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0i ProSAT]</span></td></tr>
</table>
== 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>


==Reference==
==See Also==
<ref group="xtra">PMID:023995768</ref><references group="xtra"/><references/>
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Gewirth, D T.]]
[[Category: Large Structures]]
[[Category: Seidler, P M.]]
[[Category: Gewirth DT]]
[[Category: Chaperone-inhibitor complex]]
[[Category: Seidler PM]]
[[Category: Hsp90 heat-shock protein]]
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