Proline brackets and identification of potential functional sites in proteins: Toxins to therapeutics

摘要

Protein toxins induce their specific pharmacological effects through protein-protein interaction. Identification of these protein-protein interaction sites could lead to prototypes of highly specific therapeutic agents. However, deciphering the structure-function relationships of protein toxins and locating the functional sites is a difficult, tedious and cumbersome task. We recently developed a novel predictive method to identify potential protein-protein interaction sites directly from the amino acid sequence of a protein (R. M. Kini and H. J. Evans (1996) FEES Lett. 385, 81-86) based on the presence of proline residues, a common residue found predominantly in the flanking segments of protein-protein interaction sites (R. M. Kini and H. J. Evans (1996) Biochem. Biophys. Res. Commun. 212, 1115-1124). It is a simple and straight-forward method. This review describes the new method and its application to solve structure-function relationships of protein toxins. The method is useful in identifying functional sites in toxins, despite the subtle and complex nature of their structure-function relationships and saves significant amounts of time and money. (C) 1998 Elsevier Science Ltd. All rights reserved. [References: 34]