1ha0: Difference between revisions
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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[[Image:1ha0.gif|left|200px]]<br /><applet load="1ha0" size=" | [[Image:1ha0.gif|left|200px]]<br /><applet load="1ha0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ha0, resolution 2.80Å" /> | caption="1ha0, resolution 2.80Å" /> | ||
'''HEMAGGLUTININ PRECURSOR HA0'''<br /> | '''HEMAGGLUTININ PRECURSOR HA0'''<br /> | ||
==Overview== | ==Overview== | ||
The membrane fusion potential of influenza HA, like many viral | 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 Structure== | ==About this Structure== | ||
1HA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1HA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, J.]] | [[Category: Chen, J.]] | ||
[[Category: Lee, K | [[Category: Lee, K Ho.]] | ||
[[Category: Skehel, J | [[Category: Skehel, J J.]] | ||
[[Category: Steinhauer, D | [[Category: Steinhauer, D A.]] | ||
[[Category: Stevens, D | [[Category: Stevens, D J.]] | ||
[[Category: Wiley, D | [[Category: Wiley, D C.]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:08 2008'' | ||
Revision as of 13:59, 21 February 2008
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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 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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