4ce2

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'''Unreleased structure'''
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{{STRUCTURE_4ce2| PDB=4ce2 | SCENE= }}
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===Hsp90 N-terminal domain bound to macrolactam analogues of radicicol.===
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{{ABSTRACT_PUBMED_24435512}}
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The entry 4ce2 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. 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. Required for growth at high temperatures.<ref>PMID:17114002</ref>
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Authors: Roe, S.M., Parry-Morris, S., Prodromou, C.
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==About this Structure==
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[[4ce2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CE2 OCA].
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Description: Hsp90 N-terminal domain bound to macrolactam analogues of radicicol.
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==Reference==
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<ref group="xtra">PMID:024435512</ref><references group="xtra"/><references/>
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[[Category: Parry-Morris, S.]]
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[[Category: Prodromou, C.]]
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[[Category: Roe, S M.]]
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[[Category: Chaperone]]

Revision as of 07:36, 29 January 2014

Template:STRUCTURE 4ce2

Contents

Hsp90 N-terminal domain bound to macrolactam analogues of radicicol.

Template:ABSTRACT PUBMED 24435512

Function

[HSP82_YEAST] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. 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. Required for growth at high temperatures.[1]

About this Structure

4ce2 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Dutton BL, Kitson RR, Parry-Morris S, Roe SM, Prodromou C, Moody CJ. Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90. Org Biomol Chem. 2014 Jan 17. PMID:24435512 doi:http://dx.doi.org/10.1039/c3ob42211a
  1. ↑ Proisy N, Sharp SY, Boxall K, Connelly S, Roe SM, Prodromou C, Slawin AM, Pearl LH, Workman P, Moody CJ. Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem Biol. 2006 Nov;13(11):1203-15. PMID:17114002 doi:10.1016/j.chembiol.2006.09.015

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