4o05: Difference between revisions
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{{STRUCTURE_4o05| PDB=4o05 | SCENE= }} | |||
===Identification of novel HSP90/isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's disease=== | |||
{{ABSTRACT_PUBMED_24673104}} | |||
==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> | |||
==About this Structure== | |||
[[4o05]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O05 OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024673104</ref><references group="xtra"/><references/> | |||
[[Category: Ernst, J T.]] | |||
[[Category: Zuccola, H J.]] | |||
[[Category: Chaperone]] | |||
[[Category: Chaperone-chaperone inhibitor complex]] | |||
Revision as of 09:29, 9 April 2014
Identification of novel HSP90/isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's diseaseIdentification of novel HSP90/isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's disease
Template:ABSTRACT PUBMED 24673104
FunctionFunction
[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.[1] [2]
About this StructureAbout this Structure
4o05 is a 1 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Ernst J, Neubert T, Liu M, Sperry S, Zuccola H, Turnbull A, Fleck B, Kargo W, Woody L, Chiang P, Tran D, Chen W, Snyder PW, Alcacio T, Nezami A, Reynolds J, Alvi K, Goulet L, Stamos D. Identification of novel HSP90alpha/beta isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's disease. J Med Chem. 2014 Mar 27. PMID:24673104 doi:http://dx.doi.org/10.1021/jm500042s
- ↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
- ↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200