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.
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Authors | Eva Di Silvio, Daniela Bonetti, Angelo Toto, Angela Morrone, Stefano Gianni |
Journal | Protein engineering, design & selection : PEDS
(Protein Eng Des Sel)
Vol. 27
Issue 8
Pg. 249-53
(Aug 2014)
ISSN: 1741-0134 [Electronic] England |
PMID | 24928580
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | © The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: [email protected]. |
Chemical References |
- Adenomatous Polyposis Coli Protein
- Peptides
- Protein Tyrosine Phosphatase, Non-Receptor Type 13
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Topics |
- Adenomatous Polyposis Coli Protein
(chemistry, metabolism)
- Animals
- Binding Sites
- Kinetics
- Mice
- Models, Molecular
- PDZ Domains
- Peptides
(chemistry, metabolism)
- Protein Binding
- Protein Interaction Maps
- Protein Tyrosine Phosphatase, Non-Receptor Type 13
(chemistry, metabolism)
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