Author: Subramani, Karthikeyan

Source: Current Proteomics, Volume 6, Number 3, October 2009 , pp. 198-202(5)

Publisher: Bentham Science Publishers

Abstract:

Cysteine endopeptidases regulate many physiological processes in the body and their impaired function may lead to several diseases. One of the methods of treating such diseases is achieved by controlling the proteolytic activity of these enzymes by using enzyme inhibition. This manuscript focuses on the mechanism of action of Papain, a cysteine endopeptidase enzyme and its inhibition using images generated with RasMol, which is one of the most popular graphics programs for the display of macromolecules like proteins and nucleic acid structures. The location of active site residues on the papain enzyme molecule is described with the RasMol images and the mode of inhibition of these active sites is described in reference with few examples of papain inhibitors. Thus, the manuscript discusses the use of RasMol program to understand the inhibition of cysteine endopeptidase enzyme papain.

Keywords: Papain; RasMol; cysteine; endopeptidase; enzyme; protease; inhibitors; protein data bank

Document Type: Research article

Publication date: 2009-10-01

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• Current Proteomics research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry.

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