Fiche publication
Date publication
août 2020
Journal
Structure (London, England : 1993)
Auteurs
Membres identifiés du Cancéropôle Est :
Dr GOGL Gergo
Tous les auteurs :
Ecsédi P, Gógl G, Hóf H, Kiss B, Harmat V, Nyitray L
Lien Pubmed
Résumé
To fully understand the environmental factors that influence crystallization is an enormous task, therefore crystallographers are still forced to work "blindly" trying as many crystallizing conditions and mutations to improve crystal packing as possible. Numerous times these random attempts simply fail even when using state-of-the-art techniques. As an alternative, crystallization chaperones, having good crystal-forming properties, can be invoked. Today, the almost exclusively used such protein is the maltose-binding protein (MBP) and crystallographers need other widely applicable options. Here, we introduce annexin A2 (ANXA2), which has just as good, if not better, crystal-forming ability than the wild-type MBP. Using ANXA2 as heterologous fusion partner, we were able to solve the atomic resolution structure of a challenging crystallization target, the transactivation domain (TAD) of p53 in complex with the metastasis-associated protein S100A4. p53 TAD forms an asymmetric fuzzy complex with the symmetric S1004 and could interfere with its function.
Mots clés
Ca(2+)-binding protein, MAp, PDZ domain, S100A4, X-ray crystallography, annexin A2, crystallization chaperon, metastasis, p53, protein-protein interaction
Référence
Structure. 2020 08 4;28(8):943-953.e4
