Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
IA Wilson, JJ Skehel, DC Wiley - Nature, 1981 - nature.com
IA Wilson, JJ Skehel, DC Wiley
Nature, 1981•nature.comThe haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally
distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane
and a globular region of antiparallel β-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 Å distally and folding
back to enter the membrane.
distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane
and a globular region of antiparallel β-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 Å distally and folding
back to enter the membrane.
Abstract
The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-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 Å distally and folding back to enter the membrane.
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