Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Antagonistic host-pathogen interactions offer intriguing insights into coevolutionary processes at the molecular level. Studies on secreted immune proteases from the model plant tomato and their interactions with different unrelated pathogen-derived inhibitors revealed that the inhibitors exhibit a remarkable selectivity towards different host proteases, and that the host proteases accumulate variant residues at the interaction surfaces that interfere with inhibitor binding. Here, we summarize and discuss the recent findings and use structural models to identify the molecular features underpinning protease selectivity. The observed basic principles translate to other examples of secreted immune hydrolases and their putative inhibitors.

Original publication

DOI

10.1016/j.sbi.2013.07.013

Type

Journal article

Journal

Curr Opin Struct Biol

Publication Date

12/2013

Volume

23

Pages

842 - 850

Keywords

Amino Acid Sequence, Genetic Variation, Host-Pathogen Interactions, Molecular Sequence Data, Peptide Hydrolases, Plants, Protease Inhibitors, Protein Binding