Functional dynamics of PDZ binding domains: a normal-mode analysis.

Détails

ID Serval
serval:BIB_5CD297F1B7E3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Functional dynamics of PDZ binding domains: a normal-mode analysis.
Périodique
Biophysical journal
Auteur(s)
De Los Rios P., Cecconi F., Pretre A., Dietler G., Michielin O., Piazza F., Juanico B.
ISSN
0006-3495
Statut éditorial
Publié
Date de publication
2005
Peer-reviewed
Oui
Volume
89
Numéro
1
Pages
14-21
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
Postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domains are relatively small (80-120 residues) protein binding modules central in the organization of receptor clusters and in the association of cellular proteins. Their main function is to bind C-terminals of selected proteins that are recognized through specific amino acids in their carboxyl end. Binding is associated with a deformation of the PDZ native structure and is responsible for dynamical changes in regions not in direct contact with the target. We investigate how this deformation is related to the harmonic dynamics of the PDZ structure and show that one low-frequency collective normal mode, characterized by the concerted movements of different secondary structures, is involved in the binding process. Our results suggest that even minimal structural changes are responsible for communication between distant regions of the protein, in agreement with recent NMR experiments. Thus, PDZ domains are a very clear example of how collective normal modes are able to characterize the relation between function and dynamics of proteins, and to provide indications on the precursors of binding/unbinding events.
Mots-clé
Adenosine Triphosphate/chemistry, Anisotropy, Binding Sites, Biophysics/methods, Carbon/chemistry, Crystallography, X-Ray, Guanosine Triphosphate/chemistry, Hot Temperature, Ligands, Magnetic Resonance Spectroscopy, Models, Molecular, Models, Statistical, Peptides/chemistry, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Signal Transduction, Software, Temperature, Thermodynamics
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/01/2008 12:22
Dernière modification de la notice
20/08/2019 15:15
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