5nyh
From Proteopedia
(Difference between revisions)
m (Protected "5nyh" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Hsp90-alpha N-Domain in complex with Indazole derivative== | |
| - | + | <StructureSection load='5nyh' size='340' side='right' caption='[[5nyh]], [[Resolution|resolution]] 1.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5nyh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NYH FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9EK:~{N}-methyl-~{N}-(4-morpholin-4-ylphenyl)-6-oxidanyl-3-pyrrolidin-1-ylcarbonyl-2~{H}-indazole-5-carboxamide'>9EK</scene></td></tr> | |
| - | [[ | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nyd|5nyd]]</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=5nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nyh OCA], [http://pdbe.org/5nyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nyh RCSB], [http://www.ebi.ac.uk/pdbsum/5nyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nyh ProSAT]</span></td></tr> | ||
| + | </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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Amaral, M]] | [[Category: Amaral, M]] | ||
| + | [[Category: Chaperone]] | ||
Revision as of 05:36, 18 April 2018
Crystal Structure of Hsp90-alpha N-Domain in complex with Indazole derivative
| |||||||||||
