4hy6: Difference between revisions
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{{STRUCTURE_4hy6| PDB=4hy6 | SCENE= }} | |||
===Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1=== | |||
==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== | |||
[[4hy6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HY6 OCA]. | |||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Homo sapiens]] | |||
[[Category: He, J H.]] | |||
[[Category: Li, J.]] | |||
[[Category: Yang, M.]] | |||
[[Category: Atp binding]] | |||
[[Category: Atp hydrolysis]] | |||
[[Category: Chaperone-chaperone inhibitor complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Molecular chaperone]] | |||
[[Category: Molecularchaperone]] | |||
[[Category: Rossmann fold]] | |||
Revision as of 10:31, 16 May 2013
Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1
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
4hy6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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