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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Carbohydrates / analysis
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Glycoproteins* / biosynthesis
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Hemagglutinins, Viral*
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Hydrogen Bonding
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Influenza A virus*
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Macromolecular Substances
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Membrane Proteins* / biosynthesis
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Protein Conformation
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Viral Proteins* / biosynthesis
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X-Ray Diffraction
Substances
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Carbohydrates
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Glycoproteins
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Hemagglutinins, Viral
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Macromolecular Substances
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Membrane Proteins
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Viral Proteins