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Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2818718

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

About this item

Full title

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2010-02, Vol.463 (7281), p.689-692

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Double life of flu virus protein
The current H1N1 strain pandemic virus is resistant to the established antiviral agents amantadine and rimantadine, which target the M2 protein, a multifunctional membrane-spanning proton channel. The structure of this channel has been a subject of some controversy, since an X-ray crystal structure of part of the...

Alternative Titles

Full title

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2818718

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2818718

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature08722

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