Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States

Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States

The present study provides new evidence that cationic porphyrins may be considered as tunable platforms to interfere with the structural “key code” present on the 20S proteasome α-rings and, by consequence, with its catalytic activity. Here, we describe the functional and conformational effects on t...

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Bibliographic Details
Main Authors: Anna Maria Santoro, Alessandro D’Urso, Alessandra Cunsolo, Danilo Milardi, Roberto Purrello, Diego Sbardella, Grazia R. Tundo, Donatella Diana, Roberto Fattorusso, Antonio Di Dato, Antonella Paladino, Marco Persico, Massimo Coletta, Caterina Fattorusso
Format: Article
Language:English
Published: MDPI AG 2020-09-01
Series:International Journal of Molecular Sciences
Subjects:
20S proteasome
allosteric modulator
kinetic analysis
conformational/functional equilibria
NMR studies
molecular dynamics simulation
Online Access:https://www.mdpi.com/1422-0067/21/19/7190

Internet

https://www.mdpi.com/1422-0067/21/19/7190

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