1E8T

Structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

1E8T の概要

• エントリーDOI: 10.2210/pdb1e8t/pdb
• 関連するPDBエントリー: 1E8U 1E8V
• 分子名称: HEMAGGLUTININ-NEURAMINIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: sialidase, neuraminidase, hydrolase, hemagglutinin
• 由来する生物種: Newcastle disease virus (strain Kansas)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101100.19

構造登録者

Crennell, S.,Takimoto, T.,Portner, A.,Taylor, G. (登録日: 2000-10-01, 公開日: 2001-04-03, 最終更新日: 2024-11-06)

主引用文献

Crennell, S.,Takimoto, T.,Portner, A.,Taylor, G.
Crystal Structure of the Multifunctional Paramyxovirus Hemagglutinin-Neuraminidase
Nat.Struct.Biol., 7:1068-, 2000

PubMed Abstract: Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the beta-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a beta-propeller fold. Comparison of the structures of the two complexes reveal differences in the active site, suggesting that the catalytic site is activated by a conformational switch. This site may provide both sialic acid binding and hydrolysis functions since there is no evidence for a second sialic acid binding site in HN. Evidence for a single site with dual functions is examined and supported by mutagenesis studies. The structure provides the basis for the structure-based design of inhibitors for a range of paramyxovirus-induced diseases.

PubMed: 11062565
DOI: 10.1038/81002

実験手法

X-RAY DIFFRACTION (2.5 Å)