Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 12;
Authors: Gayen A, Banigan JR, Traaseth NJ
Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms anti-parallel dimers with different monomer tilt angles relative to the lipid bilayer. In addition, subtle conformational changes were detected upon drug binding that emphasize the need for an atomic-resolution structure.
PMID: 23939862 [PubMed - as supplied by publisher]
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR
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Jonathan K. Williams, Daniel Tietze, Jun Wang, Yibing Wu, William F. DeGrado and Mei Hong
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Journal of the American Chemical Society
DOI: 10.1021/ja4041412
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[NMR paper] Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR.
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Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Linear Mode
