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Issue 3, 2015
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Electrostatic complementarity in pseudoreceptor modeling based on drug molecule crystal structures: the case of loxistatin acid (E64c)

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Abstract

After a long history of use as a prototype cysteine protease inhibitor, the crystal structure of loxistatin acid (E64c) is finally determined experimentally using intense synchrotron radiation, providing insight into how the inherent electronic nature of this protease inhibitor molecule determines its biochemical activity. Based on the striking similarity of its intermolecular interactions with those observed in a biological environment, the electrostatic potential of crystalline E64c is used to map the characteristics of a pseudo-enzyme pocket.

Graphical abstract: Electrostatic complementarity in pseudoreceptor modeling based on drug molecule crystal structures: the case of loxistatin acid (E64c)

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Article information


Submitted
05 Sep 2014
Accepted
22 Oct 2014
First published
04 Nov 2014

New J. Chem., 2015,39, 1628-1633
Article type
Paper
Author version available

Electrostatic complementarity in pseudoreceptor modeling based on drug molecule crystal structures: the case of loxistatin acid (E64c)

M. W. Shi, A. N. Sobolev, T. Schirmeister, B. Engels, T. C. Schmidt, P. Luger, S. Mebs, B. Dittrich, Y. Chen, J. M. Bąk, D. Jayatilaka, C. S. Bond, M. J. Turner, S. G. Stewart, M. A. Spackman and S. Grabowsky, New J. Chem., 2015, 39, 1628
DOI: 10.1039/C4NJ01503G

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