Linked Life Data

21081097

Source:http://linkedlifedata.com/resource/pubmed/id/21081097

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-11-18
pubmed:abstractText
NHERF1 is a multidomain scaffolding protein that assembles signaling complexes, and regulates the cell surface expression and endocytic recycling of a variety of membrane proteins. The ability of the two PDZ domains in NHERF1 to assemble protein complexes is allosterically modulated by the membrane-cytoskeleton linker protein ezrin, whose binding site is located as far as 110 Ångstroms away from the PDZ domains. Here, using neutron spin echo (NSE) spectroscopy, selective deuterium labeling, and theoretical analyses, we reveal the activation of interdomain motion in NHERF1 on nanometer length-scales and on submicrosecond timescales upon forming a complex with ezrin. We show that a much-simplified coarse-grained model suffices to describe interdomain motion of a multidomain protein or protein complex. We expect that future NSE experiments will benefit by exploiting our approach of selective deuteration to resolve the specific domain motions of interest from a plethora of global translational and rotational motions. Our results demonstrate that the dynamic propagation of allosteric signals to distal sites involves changes in long-range coupled domain motions on submicrosecond timescales, and that these coupled motions can be distinguished and characterized by NSE.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1542-0086
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
17
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3473-82
pubmed:dateRevised
2011-5-11
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy.
pubmed:affiliation
Institut Laue-Langevin, Grenoble, France.
pubmed:publicationType
Journal Article