Related Experiment Video
Updated: Apr 16, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
Published on: May 25, 2018
β-Trefoil structure enables interactions between lectins and protease inhibitors that regulate their biological
Simon Žurga1, Jure Pohleven1, Janko Kos2
1Department of Biotechnology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia; and Faculty of Pharmacy, University of Ljubljana, Aškerčeva 7, SI-1000 Ljubljana, Slovenia.
Abstract:
Fungal ricin B-like lectins and protease inhibitors, mycocypins and mycospins, are important mediators in fungal defence against antagonists and all possess the β-trefoil fold. We demonstrate here that fungal β-trefoil proteins interact with each other, in addition to their apparent targets, and that these interactions modulate their biological activity. Such regulation of carbohydrate binding or inhibitory activity is observed for the first time in β-trefoil proteins and could constitute a mechanism for regulating their physiological functions. It could also have implications in molecular recognition of other combinations of β-trefoil proteins in other species.
More Related Videos
10:33Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
Published on: October 26, 2015
08:06The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018
Related Concept Videos
Protein-protein Interfaces
Protein-Protein Interfaces
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Selectins
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...