Structure and dynamics of the influenza A M2 Channel: A comparison of three structures

Hadas Leonov, Isaiah T. Arkin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The M2 protein is an essential component of the Influenza virus' infectivity cycle. It is a homo-tetrameric bundle forming a pH-gated H+ channel. The structure of M2 was solved by three different groups, using different techniques, protein sequences and pH environment. For example, solid-state NMR spectroscopy was used on a protein in lipid bilayers, while X-ray crystallography and solution NMR spectroscopy were applied on a protein in detergent micelles. The resulting structures from the above efforts are rather distinct. Herein, we examine the different structures under uniform conditions such as a lipid bilayer and specified protonation state. We employ extensive molecular dynamics simulations, in several protonation states, representing both closed and open forms of the channel. Exploring the properties of each of these structures has shown that the X-ray structure is more stable than the other structures according to various criteria, although its water conductance and water-wire formation do not correlate to the protonation state of the channel.

Original languageAmerican English
Pages (from-to)1317-1328
Number of pages12
JournalJournal of Molecular Modeling
Volume15
Issue number11
DOIs
StatePublished - 2009

Bibliographical note

Funding Information:
This work was supported in part by grants from the Israeli science foundation (784/01,1249/05,1581/08) to ITA. ITA is the Arthur Lejwa Professor of Structural Biochemistry at the Hebrew University of Jerusalem. Molecular figures were generated using VMD.

Keywords

  • Influenza
  • Ion channel
  • Molecular dynamics
  • Protein structure

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