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Configuration Flipping in Distal Pocket of Multidrug Transporter MexB Impacts the Efflux Inhibitory Mechanism
Author(s) -
Kumar Roy Rakesh,
Patra Niladri
Publication year - 2020
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.202000947
Subject(s) - efflux , affinities , transporter , chemistry , molecular mechanics , biophysics , atp binding cassette transporter , multiple drug resistance , stereochemistry , binding affinities , quantum chemical , inhibitory postsynaptic potential , molecule , biochemistry , computational chemistry , molecular dynamics , antibiotics , biology , gene , neuroscience , organic chemistry , receptor
The Cover Feature illustrates the trimeric structure of the MexAB‐OprM efflux pump, which plays a major role in drug resistance by extruding out drugs and antibiotic molecules from cells. Using classical MD simulations, quantum mechanics/molecular mechanics, and various types of analyses, we show that D13‐9001 has a higher binding affinity towards the binding pocket compared to the experimentally determined binding affinities of D1 and D2. More information can be found in the Article by Rakesh Kumar Roy and Niladri Patra.