6olx: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "6olx" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 6olx is ON HOLD  until Paper Publication
==Hsp90-alpha S52A bound to PU-11-trans==
 
<StructureSection load='6olx' size='340' side='right'caption='[[6olx]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
Authors: Gewirth, D.T., Huck, J.D.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6olx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OLX FirstGlance]. <br>
Description: Hsp90-alpha S52A bound to PU-11-trans
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KFY:9-[(2E)-but-2-en-1-yl]-8-[(3,4,5-trimethoxyphenyl)methyl]-9H-purin-6-amine'>KFY</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n8w|6n8w]], [[6n8x|6n8x]], [[6n8y|6n8y]]</td></tr>
[[Category: Gewirth, D.T]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6olx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6olx OCA], [http://pdbe.org/6olx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6olx RCSB], [http://www.ebi.ac.uk/pdbsum/6olx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6olx ProSAT]</span></td></tr>
[[Category: Huck, J.D]]
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Gewirth, D T]]
[[Category: Huck, J D]]
[[Category: Cancer]]
[[Category: Chaperone]]
[[Category: Chaperone-chaperone inhibitor complex]]
[[Category: Cytosol]]
[[Category: Hsp90]]
[[Category: Inhibitor]]