Dynamical binding of proline-rich peptides to their recognition domains

Reference : Dynamical binding of proline-rich peptides to their recognition domains


	Document type :	Scientific journals : Other
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/10993/3771

Title :	Dynamical binding of proline-rich peptides to their recognition domains
Language :	English
Author, co-author :	Gu, Wei []
	Helms, V. [> >]
Publication date :	2005
Journal title :	Biochimica et Biophysica Acta-Proteins and Proteomics
Publisher :	Elsevier Science
Volume :	1754
Issue/season :	1-2
Special issue title :	SI
Pages :	232-238
Peer reviewed :	Yes (verified by ORBi^lu)
Audience :	International
ISSN :	1570-9639
City :	Amsterdam
Abstract :	[en] Recognition of proline-rich sequences plays an important role for the assembly of multi-protein complexes during the course of eukaryotic signal transduction and is mediated by a set of protein folds that share characteristic features. For many complex systems containing proline-rich sequences, multiple binding modes have been found by theoretical and/or experimental studies. In this review, we discuss the different binding modes as well as the correlated dynamics of the peptides and their recognition domains, and some implications to their biological functions. Further-more, we give an outlook of the systems in the context of systems biology. (c) 2005 Elsevier B.V. All rights reserved.
Permalink :	http://hdl.handle.net/10993/3771
DOI :	10.1016/j.bbapap.2005.07.033
Commentary :	JUN 25-29, 2005 4th International Conference on Inhibitors of Protein Kinases (IPK 2005) Warsaw POLAND

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