 |
 |
Journal articles
The mechanism of binding of the second PDZ domain from the Protein Tyrosine Phosphatase-BL to the Adenomatous Polyposis Coli tumor suppressor.
Abstract : Many biological processes are regulated by the interaction between protein domains and their corresponding binding partners. The PDZ domain is one of the most common protein-protein interaction modules in mammalian cells, whose role is to bind C-terminal sequences of specific targets. The second PDZ domain from the Protein Tyrosine Phosphatase-BL (PDZ2) binds to the C-terminal of Adenomatous Polyposis Coli protein (APC), one of the major tumor suppressor whose task is to regulate cell adhesion and proliferation. Here, we present a detailed kinetics analysis of the interaction between PDZ2 domain and a peptide mimicking the PDZ binding motif of APC. By analyzing data obtained at different experimental conditions, we propose a plausible mechanism for binding. Furthermore, a comparison between the dissociation rate constant measured by different methodologies allow us to identify an additional kinetic step, which is likely to arise from a conformational change of PDZ2 occurring after binding. The data are discussed on the light of previous work on PDZ domains.
Cited literature [28 references]
https://hal-riip.archives-ouvertes.fr/pasteur-01181359
Contributor : Istituto Pasteur Fondazione Cenci Bolognetti <>
Submitted on : Thursday, July 30, 2015 - 9:28:20 AM
Last modification on : Tuesday, January 28, 2020 - 11:22:14 AM
Long-term archiving on: : Saturday, October 31, 2015 - 10:21:59 AM
Contributor : Istituto Pasteur Fondazione Cenci Bolognetti <>
Submitted on : Thursday, July 30, 2015 - 9:28:20 AM
Last modification on : Tuesday, January 28, 2020 - 11:22:14 AM
Long-term archiving on: : Saturday, October 31, 2015 - 10:21:59 AM