3opd
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=3opd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3opd RCSB], [http://www.ebi.ac.uk/pdbsum/3opd 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=3opd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3opd RCSB], [http://www.ebi.ac.uk/pdbsum/3opd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HSP83_TRYBB HSP83_TRYBB]] 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 (By similarity). | ||
==See Also== | ==See Also== | ||
Revision as of 22:44, 24 December 2014
Crystal Structure of the N-terminal domain of an HSP90 from Trypanosoma Brucei, Tb10.26.1080 in the presence of a benzamide derivative
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Categories: Trypanosoma brucei brucei | Arrowsmith, C H | Bochkarev, A | Bountra, C | Chamberlain, K | Cossar, D | Edwards, A M | Fairlamb, A H | Ferguson, M A.J | Hills, T | Hui, R | Hutchinson, A | Kozieradzki, I | Li, Y | MacKenzie, C | Pizarro, J C | Structural genomic | Sullivan, H | Weadge, J | Weigelt, J | Wernimont, A K | Wyatt, P G | Atp binding | Chaperone | Sgc
