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4lwg
From Proteopedia
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==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ4== | ==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ4== | ||
<StructureSection load='4lwg' size='340' side='right' caption='[[4lwg]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4lwg' size='340' side='right' caption='[[4lwg]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FJ4:1-(5-CHLORO-2,4-DIHYDROXYPHENYL)-2-(4-METHOXYPHENYL)ETHANONE'>FJ4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FJ4:1-(5-CHLORO-2,4-DIHYDROXYPHENYL)-2-(4-METHOXYPHENYL)ETHANONE'>FJ4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lwe|4lwe]], [[4lwf|4lwf]], [[4lwh|4lwh]], [[4lwi|4lwi]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lwe|4lwe]], [[4lwf|4lwf]], [[4lwh|4lwh]], [[4lwi|4lwi]]</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=4lwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lwg RCSB], [http://www.ebi.ac.uk/pdbsum/4lwg 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=4lwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwg OCA], [http://pdbe.org/4lwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lwg RCSB], [http://www.ebi.ac.uk/pdbsum/4lwg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwg ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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> | [[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> | ||
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| + | ==See Also== | ||
| + | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:02, 4 August 2016
Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ4
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Categories: He, J | Li, J | Shi, F | Xiong, B | Atp binding | Chaperone | Molecularchaperone | Rossmann fold
