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PMID: 7464906 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.

Nature ·Vol. 289 ·No. 5796 ·1981-01-29 ·Pages 366-73

Wilson IA, Skehel JJ, Wiley DC

Abstract

The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of alpha-helices extends 76 A from the membrane and a globular region of antiparallel beta-sheet, which contains the receptor binding site and the variable antigenic determinants, is positioned on top of this stem. Each subunit has an unusual loop-like topology, starting at the membrane, extending 135 A distally and folding back to enter the membrane.

MeSH Terms
Binding Sites Carbohydrates/analysis Glycoproteins/biosynthesis Hemagglutinins, Viral Hydrogen Bonding Influenza A virus Macromolecular Substances Membrane Proteins/biosynthesis Protein Conformation Viral Proteins/biosynthesis X-Ray Diffraction
Chemicals
Carbohydrates Glycoproteins Hemagglutinins, Viral Macromolecular Substances Membrane Proteins Viral Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wilson I A
Skehel J J
Wiley D C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1981-01-29
Pages
366-73
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
NIAID NIH HHS · AI 13654 · United States
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