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  1. Progress in Biophysics and Molecular Biology
  2. Year: 2008, Volume: 98
  3. Year: 2008, Volume: 98, Issue: 1
  4. Intrinsic disorder in scaffold proteins: Getting more from less
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Dynamics of Human Atrial Cell Models: Restitution, Memory, and Intracellular Calcium Dynamics in Single Cells
Intrinsic disorder in scaffold proteins: Getting more from less
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Intrinsic disorder in scaffold proteins: Getting more from less

Content Provider PubMed Central
Author Cortese, Marc S. Uversky, Vladimir N. Dunker, A. Keith
Abstract Regulation, recognition and cell signaling involve the coordinated actions of many players. Signaling scaffolds, with their ability to bring together proteins belonging to common and/or interlinked pathways, play crucial roles in orchestrating numerous events by coordinating specific interactions among signaling proteins. This review examines the roles of intrinsic disorder (ID) in signaling scaffold protein function. Several well-characterized scaffold proteins with structurally and functionally characterized ID regions are used here to illustrate the importance of ID for scaffolding function. These examples include scaffolds that are mostly disordered, only partially disordered or those in which the ID resides in a scaffold partner. Specific scaffolds discussed include RNase, voltage-activated potassium channels, axin, BRCA1, GSK-3β, p53, Ste5, titin, Fus3, BRCA1, Titin, MAP2, D-AKAP2 and AKAP250. Among the mechanisms discussed are: molecular recognition features, fly-casting, ease of encounter complex formation, structural isolation of partners, modulation of interactions between bound partners, masking of intramolecular interaction sites, maximized interaction surface per residue, toleration of high evolutionary rates, binding site overlap, allosteric modification, palindromic binding, reduced constraints for alternative splicing, efficient regulation via posttranslational modification, efficient regulation via rapid degradation, protection of normally solvent-exposed sites, enhancing the plasticity of interaction and molecular crowding. We conclude that ID can enhance scaffold function by a diverse array of mechanisms. In other words, scaffold proteins utilize several ID-facilitated mechanisms to enhance function, and by doing so, get more functionality from less structure.
Related Links http://dx.doi.org/10.1016/j.pbiomolbio.2008.05.007
Ending Page 106
Page Count 22
Starting Page 85
File Format PDF
ISSN 00796107
Journal Progress in biophysics and molecular biology
Issue Number 1
Volume Number 98
Language English
Publisher Date 2008-09-01
Access Restriction Open
Subject Keyword Biophysics Molecular Biology Research in Higher Education
Content Type Text
Resource Type Article
Subject Molecular Biology Biophysics
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