Using sequence homology to analyze the structure and function of voltage-gated ion channel proteins.

H R Guy, S R Durell
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Abstract

Molecular modeling and mutagenesis analysis of voltage-gated channels have succeeded in identifying much of the topology of the proteins and in identifying which sequential segments are involved in functional mechanisms such as activation gating, inactivation gating, ion selectivity, and ligand binding. Efforts are currently underway to use these methods to model the protein structure and functional mechanisms more precisely. The experimental and theoretical efforts are dependent to a considerable extent upon information obtained by comparing homologous sequences. Although the fine details of models developed in this manner are unlikely to be as correct as models developed from x-ray crystallography and NMR, they still may contribute substantially to our understanding of the structure and function of these important proteins.

利用序列同源性分析了电压门控离子通道蛋白的结构和功能。
电压门控通道的分子建模和诱变分析已经成功地确定了蛋白质的大部分拓扑结构,并确定了哪些序列片段参与了诸如激活门控、失活门控、离子选择性和配体结合等功能机制。目前正在努力使用这些方法来更精确地模拟蛋白质结构和功能机制。实验和理论的努力在很大程度上依赖于通过比较同源序列获得的信息。尽管以这种方式建立的模型的细节不太可能像x射线晶体学和核磁共振建立的模型那样正确,但它们仍然可以为我们理解这些重要蛋白质的结构和功能做出重大贡献。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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