Fiche publication
Date publication
octobre 2021
Journal
Frontiers in molecular biosciences
Auteurs
Membres identifiés du Cancéropôle Est :
Dr GOGL Gergo
Tous les auteurs :
Ecsédi P, Gógl G, Nyitray L
Lien Pubmed
Résumé
S100 proteins are small, dimeric, Ca-binding proteins of considerable interest due to their associations with cancer and rheumatic and neurodegenerative diseases. They control the functions of numerous proteins by forming protein-protein complexes with them. Several of these complexes were found to display "fuzzy" properties. Examining these highly flexible interactions, however, is a difficult task, especially from a structural biology point of view. Here, we summarize the available techniques that can be deployed to obtain structural information about these dynamic complexes. We also review the current state of knowledge about the structures of S100 complexes, focusing on their often-asymmetric nature.
Mots clés
NM2A, NMR, RSK1, S100 proteins, X-ray crystallography, annexin A2, fuzzy interactions, p53
Référence
Front Mol Biosci. 2021 10 11;8:749052
