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Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2015 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 16, no 1, 64-69 p.Article in journal (Refereed) Published
Abstract [en]

PSD-95 is a scaffolding protein of the MAGUK protein family, and engages in several vital protein-protein interactions in the brain with its PDZ domains. It has been suggested that PSD-95 is composed of two supramodules, one of which is the PDZ1-2 tandem domain. Here we have developed rigidified high-affinity dimeric ligands that target the PDZ1-2 supramodule, and established the biophysical parameters of the dynamic PDZ1-2/ligand interactions. By employing ITC, protein NMR, and stopped-flow kinetics this study provides a detailed insight into the overall conformational energetics of the interaction between dimeric ligands and tandem PDZ domains. Our findings expand our understanding of the dynamics of PSD-95 with potential relevance to its biological role in interacting with multivalent receptor complexes and development of novel drugs.

Place, publisher, year, edition, pages
2015. Vol. 16, no 1, 64-69 p.
Keyword [en]
dimeric ligands, NMR spectroscopy, PDZ domains, protein-protein interactions, PSD-95
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-242373DOI: 10.1002/cbic.201402547ISI: 000346781600009OAI: oai:DiVA.org:uu-242373DiVA: diva2:783605
Available from: 2015-01-26 Created: 2015-01-26 Last updated: 2017-12-05Bibliographically approved

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Dogan, JakobJemth, Per

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