2HTR

N8 neuraminidase in complex with DANA

2HTR の概要

• エントリーDOI: 10.2210/pdb2htr/pdb
• 関連するPDBエントリー: 2HT5 2HT7 2HT8 2HTQ 2HTU 2HTV 2HTW 2HTY 2HU0 2HU4
• 分子名称: Neuraminidase, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (2 entities in total)
• 機能のキーワード: n8, neuraminidase, dana, hydrolase
• 由来する生物種: Influenza A virus
• 細胞内の位置: Virion membrane (By similarity): Q07599
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43448.77

構造登録者

Russell, R.J.,Haire, L.F.,Stevens, D.J.,Collins, P.J.,Lin, Y.P.,Blackburn, G.M.,Hay, A.J.,Gamblin, S.J.,Skehel, J.J. (登録日: 2006-07-26, 公開日: 2006-09-05, 最終更新日: 2020-07-29)

主引用文献

Russell, R.J.,Haire, L.F.,Stevens, D.J.,Collins, P.J.,Lin, Y.P.,Blackburn, G.M.,Hay, A.J.,Gamblin, S.J.,Skehel, J.J.
The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design.
Nature, 443:45-49, 2006

PubMed Abstract: The worldwide spread of H5N1 avian influenza has raised concerns that this virus might acquire the ability to pass readily among humans and cause a pandemic. Two anti-influenza drugs currently being used to treat infected patients are oseltamivir (Tamiflu) and zanamivir (Relenza), both of which target the neuraminidase enzyme of the virus. Reports of the emergence of drug resistance make the development of new anti-influenza molecules a priority. Neuraminidases from influenza type A viruses form two genetically distinct groups: group-1 contains the N1 neuraminidase of the H5N1 avian virus and group-2 contains the N2 and N9 enzymes used for the structure-based design of current drugs. Here we show by X-ray crystallography that these two groups are structurally distinct. Group-1 neuraminidases contain a cavity adjacent to their active sites that closes on ligand binding. Our analysis suggests that it may be possible to exploit the size and location of the group-1 cavity to develop new anti-influenza drugs.

PubMed: 16915235
DOI: 10.1038/nature05114

実験手法

X-RAY DIFFRACTION (2.5 Å)