View source for 3bmy


==Discovery of Benzisoxazoles as Potent Inhibitors of Chaperone Hsp90==
<StructureSection load='3bmy' size='340' side='right'caption='[[3bmy]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bmy]] 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=3BMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BMY 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXZ:4-CHLORO-6-{5-[(2-MORPHOLIN-4-YLETHYL)AMINO]-1,2-BENZISOXAZOL-3-YL}BENZENE-1,3-DIOL'>CXZ</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=3bmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bmy OCA], [https://pdbe.org/3bmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bmy RCSB], [https://www.ebi.ac.uk/pdbsum/3bmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bmy 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> 
== 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/bm/3bmy_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=3bmy ConSurf].
<div style="clear:both"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arndt K]]
[[Category: Boschelli F]]
[[Category: Chopra R]]
[[Category: Ellingboe J]]
[[Category: Golas J]]
[[Category: Gopalsamy A]]
[[Category: Jacob J]]
[[Category: Johnson J]]
[[Category: Lee F]]
[[Category: Nilakantan R]]
[[Category: Peterson R]]
[[Category: Shi M]]
[[Category: Svenson K]]
[[Category: Tam MS]]
[[Category: Vogan EM]]
[[Category: Wen Y]]