Please use this identifier to cite or link to this item:
https://hdl.handle.net/2445/138523
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 Lípids Proteïnes quinases Homologia (Biologia) Molecular models Lipids 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: https://doi.org/10.1016/j.str.2015.03.009 |
It is part of: | Structure, 2015, vol. 23, num. 5, p. 893-902 |
URI: | https://hdl.handle.net/2445/138523 |
Related resource: | https://doi.org/10.1016/j.str.2015.03.009 |
ISSN: | 0969-2126 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
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