4.3 Article Proceedings Paper

Dynamical binding of proline-rich peptides to their recognition domains

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1754, Issue 1-2, Pages 232-238

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2005.07.033

Keywords

PRS (proline-rich sequence); SH3 domain; GYF domain; WW domain; register shift; peptide binding

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.3
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available