E-mail

E-mail a Wiley Online Library Link

Malte Gersch, Felix Gut, Dr. Vadim S. Korotkov, Johannes Lehmann, Dr. Thomas Böttcher, Dr. Marion Rusch, Dr. Christian Hedberg, Prof. Dr. Herbert Waldmann, Prof. Dr. Gerhard Klebe and Prof. Dr. Stephan A. Sieber The Mechanism of Caseinolytic Protease (ClpP) Inhibition Angewandte Chemie International Edition 52

Version of Record online: 30 JAN 2013 | DOI: 10.1002/anie.201204690

Thumbnail image of graphical abstract

Catch me if you can: The ClpP protease mediates protein homeostasis and can be efficiently inhibited by β-lactones. A combination of molecular docking, mutagenesis, activity-based protein profiling, and kinetics studies now reveals the mechanism of ClpP inhibition. A hydrophobic pocket next to the active site allows binding of long aliphatic and aromatic residues. The preferred stereoisomer binds into the oxyanion hole.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field

SEARCH