FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins.

Détails

Ressource 1Télécharger: 36987846_BIB_6EA32D9B8875.pdf (1373.96 [Ko])
Etat: Public
Version: Final published version
Licence: CC BY 4.0
ID Serval
serval:BIB_6EA32D9B8875
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins.
Périodique
Nucleic acids research
Auteur⸱e⸱s
Hatos A., Teixeira JMC, Barrera-Vilarmau S., Horvath A., Tosatto SCE, Vendruscolo M., Fuxreiter M.
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Statut éditorial
Publié
Date de publication
05/07/2023
Peer-reviewed
Oui
Volume
51
Numéro
W1
Pages
W198-W206
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Proteins form complex interactions in the cellular environment to carry out their functions. They exhibit a wide range of binding modes depending on the cellular conditions, which result in a variety of ordered or disordered assemblies. To help rationalise the binding behavior of proteins, the FuzPred server predicts their sequence-based binding modes without specifying their binding partners. The binding mode defines whether the bound state is formed through a disorder-to-order transition resulting in a well-defined conformation, or through a disorder-to-disorder transition where the binding partners remain conformationally heterogeneous. To account for the context-dependent nature of the binding modes, the FuzPred method also estimates the multiplicity of binding modes, the likelihood of sampling multiple binding modes. Protein regions with a high multiplicity of binding modes may serve as regulatory sites or hot-spots for structural transitions in the assembly. To facilitate the interpretation of the predictions, protein regions with different interaction behaviors can be visualised on protein structures generated by AlphaFold. The FuzPred web server (https://fuzpred.bio.unipd.it) thus offers insights into the structural and dynamical changes of proteins upon interactions and contributes to development of structure-function relationships under a variety of cellular conditions.
Mots-clé
Protein Conformation, Proteins/chemistry, Computers, Protein Domains, Software
Pubmed
Web of science
Open Access
Oui
Création de la notice
03/04/2023 10:27
Dernière modification de la notice
08/08/2024 6:35
Données d'usage