The gates of ion channels and enzymes

被引:74
|
作者
Zhou, Huan-Xiang [1 ,2 ]
McCammon, J. Andrew [3 ,4 ,5 ]
机构
[1] Florida State Univ, Dept Phys, Tallahassee, FL 32306 USA
[2] Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA
[3] Univ Calif San Diego, Ctr Theoret Biol Phys, Dept Chem & Biochem, La Jolla, CA 92093 USA
[4] Univ Calif San Diego, Ctr Theoret Biol Phys, Dept Pharmacol, La Jolla, CA 92093 USA
[5] Univ Calif San Diego, Howard Hughes Med Inst, La Jolla, CA 92093 USA
关键词
M2 PROTON CHANNEL; MOLECULAR-DYNAMICS SIMULATION; NORMAL-MODE ANALYSIS; INFLUENZA-A VIRUS; X-RAY-STRUCTURE; CHOLESTEROL OXIDASE; GATING MECHANISM; ACETYLCHOLINE-RECEPTOR; POTASSIUM CHANNEL; CRYSTAL-STRUCTURE;
D O I
10.1016/j.tibs.2009.10.007
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
Protein dynamics are essential for virtually all protein functions, certainly for gating mechanisms of ion channels and regulation of enzyme catalysis. Ion channels usually feature a gate in the channel pore that prevents ion permeation in the closed state. Some bifunctional enzymes with two distant active sites use a tunnel to transport intermediate products; a gate can help prevent premature leakage. Enzymes with a buried active site also require a tunnel for substrate entrance; a gate along the tunnel can contribute to selectivity. The gates in these different contexts show distinct characteristics in sequence, structure and dynamics, but they also have common features. In particular, aromatic residues often appear to serve as gates, probably because of their ability, through side chain rotation, to effect large changes in cross section.
引用
收藏
页码:179 / 185
页数:7
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