1ha0

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Revision as of 17:21, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1ha0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ha0, resolution 2.80Å" /> '''HEMAGGLUTININ PRECUR...)
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File:1ha0.gif


1ha0, resolution 2.80Å

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HEMAGGLUTININ PRECURSOR HA0

OverviewOverview

The membrane fusion potential of influenza HA, like many viral, membrane-fusion glycoproteins, is generated by proteolytic cleavage of a, biosynthetic precursor. The three-dimensional structure of ectodomain of, the precursor HA0 has been determined and compared with that of cleaved, HA. The cleavage site is a prominent surface loop adjacent to a novel, cavity; cleavage results in structural rearrangements in which the, nonpolar amino acids near the new amino terminus bury ionizable residues, in the cavity that are implicated in the low-pH-induced conformational, change. Amino acid insertions at the cleavage site in HAs of virulent, avian viruses and those of viruses isolated from the recent severe, outbreak of influenza in humans in Hong Kong would extend this surface, loop, facilitating intracellular cleavage.

About this StructureAbout this Structure

1HA0 is a Single protein structure of sequence from Influenza a virus with NAG as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation., Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC, Cell. 1998 Oct 30;95(3):409-17. PMID:9814710

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