5uch
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Hsp90b N-terminal domain with inhibitors== | |
| - | + | <StructureSection load='5uch' size='340' side='right' caption='[[5uch]], [[Resolution|resolution]] 2.65Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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: | + | <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: | + | [[Category: Chaperone-inhibitor complex]] |
| - | [[Category: | + | [[Category: Hsp90]] |
| + | [[Category: Inhibitor]] | ||
Revision as of 08:26, 10 January 2018
Hsp90b N-terminal domain with inhibitors
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