6533b854fe1ef96bd12afcba
RESEARCH PRODUCT
Electrostatic complementarity in pseudoreceptor modeling based on drug molecule crystal structures: the case of loxistatin acid (E64c)
Tanja SchirmeisterThomas C. SchmidtAlexandre N. SobolevMark A. SpackmanStefan MebsBernd EngelsBirger DittrichPeter LugerYu-sheng ChenMing W. ShiDylan JayatilakaSimon GrabowskySimon GrabowskyJoanna M. BąkMichael J. TurnerCharles S. BondScott G. Stewartsubject
010405 organic chemistryChemistryIntermolecular forceGeneral ChemistryCrystal structureBiochemical Activity010402 general chemistry01 natural sciencesCysteine proteaseCatalysisProtease inhibitor (biology)0104 chemical sciencesCrystallographyLoxistatinComplementarity (molecular biology)Materials ChemistrymedicineMoleculemedicine.drugdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-01-01 | New Journal of Chemistry |