Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.

ABSTRACT: The structure and functions of the M2 protein from Influenza A are sensitive to pH, cholesterol, and the antiinfluenza drug Amantadine. This is a tetrameric membrane protein of 97 amino-acid residues that has multiple functions, among them as a proton-selective channel and facilitator of viral budding, replacing the need for the ESCRT proteins that other viruses utilize. Here, various amino-acid-specific-labeled samples of the full-length protein were prepared and mixed, so that only interresidue (13)C-(13)C cross peaks between two differently labeled proteins representing interhelical interactions are observed. This channel is activated at slightly acidic pH values in the endosome when the His(37) residues in the middle of the transmembrane domain take on a +2 or +3 charged state. Changes

SUBMITTER: Ekanayake EV 

PROVIDER: S-EPMC4816700 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature