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3wha
From Proteopedia
(Difference between revisions)
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==Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor== | ==Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor== | ||
<StructureSection load='3wha' size='340' side='right' caption='[[3wha]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='3wha' size='340' side='right' caption='[[3wha]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b28|3b28]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b28|3b28]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wha OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wha RCSB], [http://www.ebi.ac.uk/pdbsum/3wha 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=3wha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wha OCA], [http://pdbe.org/3wha PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wha RCSB], [http://www.ebi.ac.uk/pdbsum/3wha PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wha ProSAT]</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 == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3wha" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:28, 5 August 2016
Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor
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