H2N2V1, PubMed, Corpus, bibRecord, 000372

Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.

Identifieur interne : 000372 ( PubMed/Corpus ); précédent : 000371; suivant : 000373

Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.

Auteurs : C. Böttcher ; K. Ludwig ; A. Herrmann ; M. Van Heel ; H. Stark

Source :

FEBS letters [ 0014-5793 ] ; 1999.

RBID : pubmed:10606732

English descriptors

KwdEn :
- Cryoelectron Microscopy, Hemagglutinins, Viral (chemistry), Hemagglutinins, Viral (ultrastructure), Hydrogen-Ion Concentration, Influenza A virus (chemistry), Models, Molecular, Protein Conformation.
MESH :
- chemical , chemistry : Hemagglutinins, Viral.
- chemical , ultrastructure : Hemagglutinins, Viral.
- chemistry : Influenza A virus.
- Cryoelectron Microscopy, Hydrogen-Ion Concentration, Models, Molecular, Protein Conformation.

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 A and 14 A, 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.

DOI: 10.1016/s0014-5793(99)01475-1
PubMed: 10606732

Links to Exploration step

pubmed:10606732

Le document en format XML

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<author><name sortKey="Bottcher, C" sort="Bottcher, C" uniqKey="Bottcher C" first="C" last="Böttcher">C. Böttcher</name>
<affiliation><nlm:affiliation>Freie Universität Berlin, Institut für Chemie/Forschungszentrum für Elektronenmikroskopie, Fabeckstr. 36a, D-14195, Berlin, Germany.</nlm:affiliation>
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<author><name sortKey="Ludwig, K" sort="Ludwig, K" uniqKey="Ludwig K" first="K" last="Ludwig">K. Ludwig</name>
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<author><name sortKey="Herrmann, A" sort="Herrmann, A" uniqKey="Herrmann A" first="A" last="Herrmann">A. Herrmann</name>
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<author><name sortKey="Van Heel, M" sort="Van Heel, M" uniqKey="Van Heel M" first="M" last="Van Heel">M. Van Heel</name>
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<author><name sortKey="Stark, H" sort="Stark, H" uniqKey="Stark H" first="H" last="Stark">H. Stark</name>
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<author><name sortKey="Bottcher, C" sort="Bottcher, C" uniqKey="Bottcher C" first="C" last="Böttcher">C. Böttcher</name>
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<author><name sortKey="Ludwig, K" sort="Ludwig, K" uniqKey="Ludwig K" first="K" last="Ludwig">K. Ludwig</name>
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<term>Hydrogen-Ion Concentration</term>
<term>Influenza A virus (chemistry)</term>
<term>Models, Molecular</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A virus</term>
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<front><div type="abstract" xml:lang="en">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 A and 14 A, 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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<Abstract><AbstractText>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 A and 14 A, 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.</AbstractText>
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Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.

Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki