5uch: Difference between revisions

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'''Unreleased structure'''


The entry 5uch is ON HOLD  until Paper Publication
==Hsp90b N-terminal domain with inhibitors==
 
<StructureSection load='5uch' size='340' side='right' caption='[[5uch]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
Authors: Peng, S., Balch, M., Matts, R., Deng, J.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5uch]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCH FirstGlance]. <br>
Description: Hsp90b N-terminal domain with inhibitors
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=871:2-(5-Hydroxy-4-(isoindoline-2-carbonyl)-2-isopropylphenyl)acetonitrile'>871</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uci|5uci]], [[5ucj|5ucj]]</td></tr>
<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=5uch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uch OCA], [http://pdbe.org/5uch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uch RCSB], [http://www.ebi.ac.uk/pdbsum/5uch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uch ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/HS90B_HUMAN HS90B_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:16478993</ref> <ref>PMID:19696785</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Balch, M]]
[[Category: Deng, J]]
[[Category: Deng, J]]
[[Category: Matts, R]]
[[Category: Peng, S]]
[[Category: Peng, S]]
[[Category: Matts, R]]
[[Category: Chaperone-inhibitor complex]]
[[Category: Balch, M]]
[[Category: Hsp90]]
[[Category: Inhibitor]]