The gramicidin ion channel: A model membrane protein

被引：286

作者：

Kelkar, Devaki A. ^{[1
]}

Chattopadhyay, Amitabha ^{[1
]}

机构：

[1] Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2007年 / 1768卷 / 09期

关键词：

gramicidin; ion channel; tryptophan; membrane interface; lipid-protein interaction; HII PHASE-FORMATION; SOLID-STATE NMR; WAVELENGTH-SELECTIVE FLUORESCENCE; MOLECULAR-DYNAMICS SIMULATIONS; DIOXOLANE-LINKED GRAMICIDIN; LIPID-BILAYER ENVIRONMENT; A TRANSMEMBRANE CHANNEL; AMINO-ACID-SEQUENCE; X-RAY-STRUCTURE; HYDROPHOBIC MISMATCH;

D O I：

10.1016/j.bbamem.2007.05.011

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 linear peptide gramicidin forms prototypical ion channels specific for monovalent cations and has been extensively used to study the organization, dynamics and function of membrane-spanning channels. In recent times, the availability of crystal structures of complex ion channels has challenged the role of gramicidin as a model membrane protein and ion channel. This review focuses on the suitability of gramicidin as a model membrane protein in general, and the information gained from gramicidin to understand lipid-protein interactions in particular. Special emphasis is given to the role and orientation of tryptophan residues in channel structure and function and recent spectroscopic approaches that have highlighted the organization and dynamics of the channel in membrane and membrane-mimetic media. (C) 2007 Elsevier B.V. All rights reserved.

引用

页码：2011 / 2025

页数：15

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