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Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases*

Identifieur interne : 000852 ( Main/Exploration ); précédent : 000851; suivant : 000853

Polar Residues and Their Positional Context Dictate the Transmembrane Domain Interactions of Influenza A Neuraminidases*

Auteurs : Johan Nordholm [Suède] ; Diogo V. Da Silva [Suède] ; Justina Damjanovic [Suède] ; Dan Dou [Suède] ; Robert Daniels [Suède]

Source :

RBID : PMC:3624445

Abstract

Background: Transmembrane domain (TMD) interactions in bitopic proteins are less understood than in multispanning proteins.

Results: The interaction of the neuraminidase TMDs from influenza A viruses increases with decreasing hydrophobicity.

Conclusion: Neuraminidase TMD interactions are dependent on the helix localization and positioning of their polar residues in the membrane bilayer.

Significance: Polar-mediated TMD interactions are related to their membrane-integration properties.


Url:
DOI: 10.1074/jbc.M112.440230
PubMed: 23447533
PubMed Central: 3624445


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<bold>Background:</bold>
Transmembrane domain (TMD) interactions in bitopic proteins are less understood than in multispanning proteins.</p>
<p>
<bold>Results:</bold>
The interaction of the neuraminidase TMDs from influenza A viruses increases with decreasing hydrophobicity.</p>
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<bold>Conclusion:</bold>
Neuraminidase TMD interactions are dependent on the helix localization and positioning of their polar residues in the membrane bilayer.</p>
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Polar-mediated TMD interactions are related to their membrane-integration properties.</p>
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