3b26
From Proteopedia
(Difference between revisions)
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<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=3b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b26 RCSB], [http://www.ebi.ac.uk/pdbsum/3b26 PDBsum]</span></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=3b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b26 RCSB], [http://www.ebi.ac.uk/pdbsum/3b26 PDBsum]</span></td></tr> | ||
</table> | </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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 23:15, 24 December 2014
Hsp90 alpha N-terminal domain in complex with an inhibitor Ro1127850
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