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Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System

Bunney, Tom D., Inglis, Alison J., Sanfelice, Domenico, Farrell, Brendan, Kerr, Christopher J., Thompson, Gary S., Masson, Glenn R., Thiyagarajan, Nethaji, Svergun, Dmitri I., Williams, Roger L., and others. (2018) Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System. Structure, 26 (3). pp. 446-458. ISSN 0969-2126. (doi:10.1016/j.str.2018.01.016) (KAR id:66869)

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https://doi.org/10.1016/j.str.2018.01.016

Abstract

Receptor tyrosine kinase FGFR3 is involved in many

developmental disorders and cancer. The Hsp90/

normal and neoplastic cells. Here we uncover the

teins by combining approaches including NMR,

linked mutations convert FGFR3 to a stronger client,

involves an allosteric network through the N-lobe

ture of the client kinase/Cdc37 complex and dem on-

binding of Cdc37 to unrelated kinases induces a

the kinase N-lobe, beyond localized changes and in-

shown for FGFR3, this processing by Cdc37 deacti-

tion established in the complex, for direct recognition

by Hsp90.

Item Type: Article
DOI/Identification number: 10.1016/j.str.2018.01.016
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Gary Thompson
Date Deposited: 30 Apr 2018 11:00 UTC
Last Modified: 29 May 2019 20:30 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/66869 (The current URI for this page, for reference purposes)
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