Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling.

ABSTRACT: As a target of antiviral drugs, the influenza A M2 protein has been the focus of numerous structural studies and has been extensively explored as a model ion channel. In this study, we capitalize on the expanding body of high-resolution structural data available for the M2 protein to design and interpret site-directed spin-labeling electron paramagnetic resonance spectroscopy experiments on drug-induced conformational changes of the M2 protein embedded in lipid bilayers. We obtained data in the presence of adamantane drugs for two different M2 constructs (M2TM 22-46 and M2TMC 23-60). M2TM peptides were spin labeled at the N-terminal end of the transmembrane domain. M2TMC peptides were spin labeled site specifically at cysteine residues substituted for amino acids within the transmembrane d

SUBMITTER: Thomaston JL 

PROVIDER: S-EPMC3575861 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature