1HA0

HEMAGGLUTININ PRECURSOR HA0

1HA0 の概要

• エントリーDOI: 10.2210/pdb1ha0/pdb
• 分子名称: 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)
• 機能のキーワード: glycoprotein, membrane-fusion precursor, virus/viral protein, viral protein
• 由来する生物種: Influenza A virus
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (Potential): P03437
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57548.83

構造登録者

Chen, J.,Ho Lee, K.,Steinhauer, D.A.,Stevens, D.J.,Skehel, J.J.,Wiley, D.C. (登録日: 1998-10-08, 公開日: 1998-10-12, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)