2ye3: 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=2ye3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ye3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ye3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ye3 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=2ye3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ye3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ye3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ye3 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> | |||
==See Also== | |||
*[[Heat Shock Proteins|Heat Shock Proteins]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Baker, L M | [[Category: Baker, L M]] | ||
[[Category: Hubbard, R E | [[Category: Hubbard, R E]] | ||
[[Category: Roughley, S D | [[Category: Roughley, S D]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Atpase]] | [[Category: Atpase]] | ||
Revision as of 18:52, 24 December 2014
HSP90 INHIBITORS AND DRUGS FROM FRAGMENT AND VIRTUAL SCREENINGHSP90 INHIBITORS AND DRUGS FROM FRAGMENT AND VIRTUAL SCREENING
Structural highlights
Function[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.[1] [2] See AlsoReferences
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