Viral channel forming proteins - Modeling the target

被引：33

作者：

Fischer, Wolfgang B. ^{[1
]}

Hsu, Hao-Jen ^{[1
]}

机构：

[1] Natl Yang Ming Univ, Sch Biomed Sci & Engn, Inst Biophoton, Taipei 112, Taiwan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2011年 / 1808卷 / 02期

关键词：

Viral channel protein; Assembly; Docking; Sequence alignment; Ion channel; Toxin; HEPATITIS-C-VIRUS; INFLUENZA-A VIRUS; M2 PROTON CHANNEL; ION-CHANNEL; TRANSMEMBRANE PEPTIDE; P7; PROTEIN; MEMBRANE PERMEABILIZATION; POTASSIUM CHANNEL; HIV-1; VPU; B VIRUS;

D O I：

10.1016/j.bbamem.2010.05.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cellular and subcellular membranes encounter an important playground for the activity of membrane proteins encoded by viruses. Viral membrane proteins, similar to their host companions, can be integral or attached to the membrane. They are involved in directing the cellular and viral reproduction, the fusion and budding processes. This review focuses especially on those integral viral membrane proteins which form channels or pores, the classification to be so. modeling by in silico methods and potential drug candidates. The sequence of an isolate of Vpu from HIV-1 is aligned with host ion channels and a toxin. The focus is on the alignment of the transmembrane domains. The results of the alignment are mapped onto the 3D structures of the respective channels and toxin. The results of the mapping support the idea of a 'channel-pore dualism' for Vpu. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：561 / 571

页数：11

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