Issue 46, 2018
From the journal:

Chemical Communications

Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures†

Yue Liu,a   Junjun Tan,a   Jiahui Zhang,a   Chuanzhao Li,a   Yi Luoa  and  Shuji Ye ORCID logo *a  

* Corresponding authors

a Hefei National Laboratory for Physical Sciences at the Microscale, and Synergetic Innovation Center for Quantum Information & Quantum Physics, University of Science and Technology of China, Hefei, Anhui 230026, China
E-mail: shujiye@ustc.edu.cn

Abstract

We discovered for the first time that the influenza A virus M2TM tunes its conformational heterogeneity and structural plasticity to respond to environmental cues by undergoing a helix-to-loop transition, resolving controversies regarding the mechanism of proton conduction and plasticity of the M2TM in lipid bilayers.

Graphical abstract: Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures

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Article information

DOI
https://doi.org/10.1039/C8CC01533C
Article type
Communication
Submitted
24 Feb 2018
Accepted
11 May 2018
First published
11 May 2018

Chem. Commun., 2018,54, 5903-5906

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Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures

Y. Liu, J. Tan, J. Zhang, C. Li, Y. Luo and S. Ye, Chem. Commun., 2018, 54, 5903 DOI: 10.1039/C8CC01533C

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