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

Ming W. Shi, Alexandre N. Sobolev, Tanja Schirmeister, Bernd Engels, Thomas C. Schmidt, Peter Luger, Stefan Mebs, Birger Dittrich, Yu Sheng Chen, Joanna M. Bąk, Dylan Jayatilaka, Charles S. Bond, Michael J. Turner, Scott G. Stewart, Mark A. Spackman, Simon Grabowsky

Research output: Contribution to journalArticlepeer-review

10 Citations (Web of Science)
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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.

Original languageEnglish
Pages (from-to)1628-1633
Number of pages6
JournalNew Journal of Chemistry
Volume39
Issue number3
DOIs
Publication statusPublished - 1 Mar 2015

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