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2HTV

N4 neuraminidase

2HTV の概要
エントリーDOI10.2210/pdb2htv/pdb
関連するPDBエントリー2HT5 2HT7 2HT8 2HTQ 2HTR 2HTU 2HTW 2HTY 2HU0 2HU4
分子名称Neuraminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
機能のキーワードn4, neuraminidase, hydrolase
由来する生物種Influenza A virus
タンパク質・核酸の鎖数2
化学式量合計86388.56
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: 2024-11-20)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 2htv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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