1HA0

HEMAGGLUTININ PRECURSOR HA0

Summary for 1HA0

• Entry DOI: 10.2210/pdb1ha0/pdb
• Descriptor: PROTEIN (HEMAGGLUTININ PRECURSOR), beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: glycoprotein, membrane-fusion precursor, virus/viral protein, viral protein
• Biological source: Influenza A virus
• Cellular location: Virion membrane; Single-pass type I membrane protein (Potential): P03437
• Total number of polymer chains: 1
• Total formula weight: 57548.83

Authors

Chen, J.,Ho Lee, K.,Steinhauer, D.A.,Stevens, D.J.,Skehel, J.J.,Wiley, D.C. (deposition date: 1998-10-08, release date: 1998-10-12, Last modification date: 2024-10-16)

Primary citation

Chen, J.,Lee, K.H.,Steinhauer, D.A.,Stevens, D.J.,Skehel, J.J.,Wiley, D.C.
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation.
Cell(Cambridge,Mass.), 95:409-417, 1998

PubMed Abstract: 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.

PubMed: 9814710
DOI: 10.1016/S0092-8674(00)81771-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)