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[[Image:1yes.png|left|200px]]


{{STRUCTURE_1yes|  PDB=1yes  |  SCENE=  }}
==HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION==
 
<StructureSection load='1yes' size='340' side='right'caption='[[1yes]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
===HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1yes]] 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=1YES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YES FirstGlance]. <br>
{{ABSTRACT_PUBMED_9108479}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1yes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yes OCA], [https://pdbe.org/1yes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yes RCSB], [https://www.ebi.ac.uk/pdbsum/1yes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yes ProSAT]</span></td></tr>
==About this Structure==
</table>
[[1yes]] is a 1 chain structure of [[Heat Shock Proteins]] 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=1YES OCA].  
== 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ye/1yes_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yes ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:009108479</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Pavletich, N P.]]
[[Category: Large Structures]]
[[Category: Russo, A A.]]
[[Category: Pavletich NP]]
[[Category: Stebbins, C E.]]
[[Category: Russo AA]]
[[Category: Chaperone protein]]
[[Category: Stebbins CE]]
[[Category: Geldanamycin]]
[[Category: Heat shock]]
[[Category: Signal transduction]]
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