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Article

pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.

Proceedings of the National Academy of Sciences of the United States of America - 4 Dec 2012

Lorieau Justin L, Louis John M, Schwieters Charles D, Bax Adriaan

Abstract excerpt

The highly conserved first 23 residues of the influenza hemagglutinin HA2 subunit constitute the fusion domain, which plays a pivotal role in fusing viral and host-cell membranes. At neutral pH, this peptide adopts a tight helical hairpin wedge structure, stabilized by aliphatic hydrogen bonding and charge-dipole interactions. We demonstrate that at low pH, where the fusion process is triggered, the native...

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Share to Amino Acid Sequence
Share to Hemagglutinins, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

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Share to Nuclear Magnetic Resonance, Biomolecular

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Identifiers

PMID: 23169643
DOI: 10.1073/pnas.1213801109
PMCID: PMC3523815

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