Dynamical binding of proline-rich peptides to their recognition domains.
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. Furthermore, we give an outlook of the systems in the context of systems biology.
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Zentrum für Bioinformatik, Universität des Saarlandes, D-66041 Saarbrücken, Germany.
Helms
Volkhard
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D008024:Ligands; D008954:Models, Biological; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011392:Proline / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D008024:Ligands; D010455:Peptides; D011392:Proline