4hy6

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'''Unreleased structure'''
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{{STRUCTURE_4hy6| PDB=4hy6 | SCENE= }}
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===Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1===
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The entry 4hy6 is ON HOLD until May 13 2014
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==Function==
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[[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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Authors: Yang, M., Li, J., He, J.H.
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==About this Structure==
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[[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].
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Description: Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: He, J H.]]
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[[Category: Li, J.]]
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[[Category: Yang, M.]]
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[[Category: Atp binding]]
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[[Category: Atp hydrolysis]]
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[[Category: Chaperone-chaperone inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: Molecular chaperone]]
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[[Category: Molecularchaperone]]
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[[Category: Rossmann fold]]

Revision as of 07:31, 16 May 2013

Template:STRUCTURE 4hy6

Contents

Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ1

Function

[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 Structure

4hy6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. ↑ 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
  2. ↑ 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

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