4ykt
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Heat Shock Protein 90 Bound to CS307== | |
| - | + | <StructureSection load='4ykt' size='340' side='right' caption='[[4ykt]], [[Resolution|resolution]] 1.85Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ykt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YKT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4EQ:1-(5-CHLORO-2,4-DIHYDROXYPHENYL)-5-({[DIHYDROXY(PYRIDIN-3-YL)-LAMBDA~4~-SULFANYL]AMINO}METHYL)-1,3-DIHYDRO-2H-BENZIMIDAZOL-2-ONE'>4EQ</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ykq|4ykq]], [[4ykr|4ykr]], [[4yku|4yku]], [[4ykw|4ykw]], [[4ykx|4ykx]], [[4yky|4yky]], [[4ykz|4ykz]]</td></tr> |
| - | [[Category: Stuckey, J | + | <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=4ykt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ykt OCA], [http://pdbe.org/4ykt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ykt RCSB], [http://www.ebi.ac.uk/pdbsum/4ykt PDBsum]</span></td></tr> |
| - | [[Category: | + | </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: Kang, Y N]] | ||
| + | [[Category: Stuckey, J A]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Chaperone-inhibitor complex]] | ||
| + | [[Category: Hsp 90]] | ||
| + | [[Category: Protein-inhibitor complex]] | ||
Revision as of 03:49, 10 March 2016
Heat Shock Protein 90 Bound to CS307
| |||||||||||
