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4nh8

From Proteopedia

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'''Unreleased structure'''
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{{STRUCTURE_4nh8| PDB=4nh8 | SCENE= }}
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===Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity===
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{{ABSTRACT_PUBMED_24332488}}
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The entry 4nh8 is ON HOLD
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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: Ernst, J.T., Zuccola, H.J.
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==About this Structure==
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[[4nh8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NH8 OCA].
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Description: Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity
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==Reference==
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<ref group="xtra">PMID:024332488</ref><references group="xtra"/><references/>
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[[Category: Ernst, J T.]]
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[[Category: Zuccola, H J.]]
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[[Category: A/b protein]]
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[[Category: Chaperone]]

Revision as of 08:12, 15 January 2014

Template:STRUCTURE 4nh8

Contents

Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity

Template:ABSTRACT PUBMED 24332488

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

4nh8 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Ernst JT, Liu M, Zuccola H, Neubert T, Beaumont K, Turnbull A, Kallel A, Vought B, Stamos D. Correlation between chemotype-dependent binding conformations of HSP90alpha/beta and isoform selectivity-Implications for the structure-based design of HSP90alpha/beta selective inhibitors for treating neurodegenerative diseases. Bioorg Med Chem Lett. 2014 Jan 1;24(1):204-8. doi: 10.1016/j.bmcl.2013.11.036., Epub 2013 Nov 23. PMID:24332488 doi:http://dx.doi.org/10.1016/j.bmcl.2013.11.036
  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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