The mechanism of binding of the second PDZ domain from the Protein Tyrosine Phosphatase-BL to the Adenomatous Polyposis Coli tumor suppressor
| Autor: | Eva Di Silvio, Stefano Gianni, Angela Morrone, Daniela Bonetti, Angelo Toto |
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| Přispěvatelé: | Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Department of Chemistry [Cambridge, UK], University of Cambridge [UK] (CAM), This work partly supported by grants from the Italian Ministero dell’Istruzionedell’Universita` e della Ricerca (Progetto di Interesse ‘Invecchiamento’ toS.G.) and Sapienza University of Rome (C26A13T9NB to S.G.). |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular MESH: Adenomatous Polyposis Coli Protein Adenomatous polyposis coli Adenomatous Polyposis Coli Protein Protein domain PDZ domain Protein Tyrosine Phosphatase Non-Receptor Type 13 PDZ Domains Bioengineering Peptide binding Protein tyrosine phosphatase Non-Receptor Type 13 Biochemistry Protein–protein interaction protein-protein interaction Mice Models MESH: PDZ Domains Animals MESH: Protein Binding MESH: Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Protein Interaction Maps Tyrosine Molecular Biology MESH: Mice MESH: Protein Interaction Maps Binding Sites biology MESH: Kinetics MESH: Peptides Medicine (all) Molecular Cell biology Kinetics MESH: Binding Sites biology.protein Peptides Protein Binding Biotechnology Protein Tyrosine Phosphatase MESH: Protein Tyrosine Phosphatase Non-Receptor Type 13 MESH: Models Molecular Binding domain |
| Zdroj: | Protein Engineering, Design and Selection Protein Engineering, Design and Selection, Oxford University Press (OUP), 2014, 27 (8), pp.249-53. ⟨10.1093/protein/gzu022⟩ |
| ISSN: | 1741-0126 1741-0134 |
| DOI: | 10.1093/protein/gzu022⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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