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PMID: 9370444 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation.

Biophysical journal ·Vol. 73 ·No. 5 ·1997-11-00 ·Pages 2511-7

Kovacs FA, Cross TA

Abstract

The transmembrane portion of the M2 protein from the Influenza A virus has been studied in hydrated dimyristroylphosphotidylcholine lipid bilayers with solid-state NMR. Orientational constraints were obtained from isotopically labeled peptide samples mechanically aligned between thin glass plates. 15N chemical shifts from single site labeled samples constrain the molecular frame with respect to the magnetic field. When these constraints are applied to the peptide, modeled as a uniform alpha-helix, the tilt of the helix with respect to the bilayer normal was determined to be 33 degrees +/- 3 degrees. Furthermore, the orientation about the helix axis was also determined within an error of +/- 30 degrees. These results imply that the packing of this tetrameric protein is in a left-handed four-helix bundle. Only with such a large tilt angle are the hydrophilic residues aligned to the channel axis.

MeSH Terms
Amino Acid Sequence Influenza A virus/chemistry Ion Channels/chemistry Magnetic Resonance Spectroscopy Membrane Proteins/chemistry Models, Molecular Molecular Sequence Data Peptide Fragments/chemical synthesis,chemistry Protein Structure, Secondary Viral Matrix Proteins/chemistry,metabolism
Chemicals
Ion Channels M-protein, influenza virus M2 protein, Influenza A virus Membrane Proteins Peptide Fragments Viral Matrix Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kovacs F A
Institute of Molecular Biophysics and Department of Chemistry, Florida State University, Tallahassee 32306-4005, USA.
Cross T A
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(97)78279-1
Published
1997-11-00
Pages
2511-7
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1181152
Subset
IM
External Links
PubMed source DOI: 10.1016/S0006-3495(97)78279-1 PMC Full Text View journal details
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