Neutron spin echo spectroscopy study of the dynamics of a multi-domain protein with an intrinsically disordered domain

DOI

Previous studies have shown that ezrin binding to the scaffolding proteins NHERF1, allosterically activates the PDZ domains of NHERF1 to interact with target proteins. Biochemical and cell biological studies have shown that phosphorylation of NHERF1 reduces the ability of NHERF1 to assemble protein complexes in cells. Here we propose to use NSE to determine the effects of phosphorylation of S339 and S340 on the domain motion in NHERF1 and in the NHERF1∙Ezrin complex

Identifier
DOI https://doi.org/10.5291/ILL-DATA.8-04-749
Metadata Access https://data.ill.fr/openaire/oai?verb=GetRecord&metadataPrefix=oai_datacite&identifier=10.5291/ILL-DATA.8-04-749
Provenance
Creator Farago, Bela; Callaway, David; Nicholl, Iain; Bu, Zimei
Publisher Institut Laue-Langevin
Publication Year 2017
Rights OpenAccess; info:eu-repo/semantics/openAccess
OpenAccess true
Representation
Resource Type Dataset
Size 378 MB
Version 1
Discipline Particles, Nuclei and Fields