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==Hsp90b N-terminal domain with inhibitors== | |||
<StructureSection load='5uci' size='340' side='right' caption='[[5uci]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5uci]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=874:(2,4-Dihydroxy-3-(hydroxymethyl)-5-isopropylphenyl)(isoindolin-2-yl)methanone'>874</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uch|5uch]], [[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=5uci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uci OCA], [http://pdbe.org/5uci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uci RCSB], [http://www.ebi.ac.uk/pdbsum/5uci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uci 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: | [[Category: Chaperone-inhibitor complex]] | ||
[[Category: | [[Category: Hsp90 inhibitor]] |
Revision as of 08:45, 3 January 2018
Hsp90b N-terminal domain with inhibitorsHsp90b N-terminal domain with inhibitors
Structural highlights
Function[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.[1] [2] References
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