Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone 13CO-15N rotational-echo double-resonance solid-state NMR

Journal of Biomolecular NMR - Tập 55 - Trang 139-146 - 2013
Ujjayini Ghosh1, Li Xie1, David P. Weliky1
1Department of Chemistry, Michigan State University, East Lansing, USA

Tóm tắt

The influenza virus fusion peptide is the N-terminal ~20 residues of the HA2 subunit of the hemagglutinin protein and this peptide plays a key role in the fusion of the viral and endosomal membranes during initial infection of a cell. The fusion peptide adopts N-helix/turn/C-helix structure in both detergent and membranes with reports of both open and closed interhelical topologies. In the present study, backbone 13CO-15N REDOR solid-state NMR was applied to the membrane-associated fusion peptide to detect the distribution of interhelical distances. The data clearly showed a large fraction of closed and semi-closed topologies and were best-fitted to a mixture of two structures that do not exchange. One of the earlier open structural models may have incorrect G13 dihedral angles derived from TALOS analysis of experimentally correct 13C shifts.

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