Please use this identifier to cite or link to this item:
Title: The SH3 domain acts as a scaffold for the N-terminal intrinsically disordered regions of c-Src
Author: Maffei, Mariano, 1985-
Arbesú Andrés, Miguel
Le Roux, Anabel-Lise
Amata, Irene
Roche, Serge
Pons Vallès, Miquel
Keywords: Models moleculars
Proteïnes quinases
Homologia (Biologia)
Molecular models
Protein kinases
Homology (Biology)
Issue Date: 23-Apr-2015
Publisher: Elsevier Ltd
Abstract: Regulation of c-Src activity by the intrinsically disordered Unique domain has been recently demonstrated. However, its connection with the classical regulatory mechanisms is still missing. Here we show that the Unique domain is part of a long loop closed by the interaction of the SH4 and SH3 domains. The conformational freedom of the Unique domain is further restricted through direct contacts with SH3 that are allosterically modulated by binding of a poly-proline ligand in the presence and in the absence of lipids. Our results highlight the scaffolding role of the SH3 domain for the c-Src N-terminal intrinsically disordered regions and suggest a connection between the regulatory mechanisms involving the SH3 and Unique domains.
Note: Versió postprint del document publicat a:
It is part of: Structure, 2015, vol. 23, num. 5, p. 893-902
Related resource:
ISSN: 0969-2126
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

Files in This Item:
File Description SizeFormat 
651266.pdf1.56 MBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.