Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
Identifieur interne : 001A34 ( Main/Merge ); précédent : 001A33; suivant : 001A35Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
Auteurs : Christoph Böttcher [Allemagne] ; Kai Ludwig [Allemagne] ; Andreas Herrmann [Allemagne] ; Marin Van Heel [Royaume-Uni] ; Holger Stark [Allemagne]Source :
- FEBS Letters [ 0014-5793 ] ; 1999.
English descriptors
- Teeft :
- Acidic, Angular approach, Angular reconstitution, Biol, Cell biol, Central cavity, Cold spring harb, Conformation, Conformational, Conformational change, Conformational states, Conformational transitions, Crystallographic structure, Digitised micrographs, Distal domains, Ectodomain, Entire ectodomain, Feb, Fourier shell correlation, Fourier space, Fusion capacity, Fusion peptide, Fusion sequence, Geel zwart, Haemagglutinin, Haemagglutinin trimer, Image processing procedure, Individual trimers, Loop region, Membrane, Micrographs, Projection images, Rosette, Skehel, Subunit, Target membrane, Target membranes, Trimer, Trimeric ectodomain, Viral, Viral membrane, Whole trimer.
Abstract
Abstract: The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.
Url:
DOI: 10.1016/S0014-5793(99)01475-1
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<term>Central cavity</term>
<term>Cold spring harb</term>
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<term>Conformational</term>
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<term>Conformational transitions</term>
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<front><div type="abstract" xml:lang="en">Abstract: The three-dimensional structures of the complete haemagglutinin (HA) of influenza virus A/Japan/305/57 (H2N2) in its native (neutral pH) and membrane fusion-competent (low pH) form by electron cryo-microscopy at a resolution of 10 Å and 14 Å, respectively, have been determined. In the fusion-competent form the subunits remain closely associated preserving typical overall features of the trimeric ectodomain at neutral pH. Rearrangements of the tertiary structure in the distal and the stem parts are associated with the formation of a central cavity through the entire ectodomain. We suggest that the cavity is essential for relocation of the so-called fusion sequence of HA towards the target membrane.</div>
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