3mnr
From Proteopedia
(Difference between revisions)
| Line 7: | Line 7: | ||
<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=3mnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mnr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mnr RCSB], [http://www.ebi.ac.uk/pdbsum/3mnr 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=3mnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mnr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mnr RCSB], [http://www.ebi.ac.uk/pdbsum/3mnr 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:03, 25 December 2014
Crystal Structure of Benzamide SNX-1321 bound to Hsp90
| |||||||||||
