POTASSIUM CHANNEL SELECTIVITY FILTER

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 本项目的长期目标是通过对KCSA和KvAP中K+通道门控的分析，进一步了解电压依赖通道门控的分子机制。对原核生物钾通道KCSA中pH传感器的分子同一性分析确定了几个关键突变体，它们在中性pH下稳定了KCSA内束门的全开放构象，这一事实使KCSA在各种功能状态下的结晶学分析成为可能。选择性过滤器中的其他突变被设计用于确定通道的完全传导和失活形式以及模式门控事件的探测。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The long-term goal of this project is to further understand the molecular mechanisms of gating in voltage-dependent channels, by focusing on the analysis of K+ channel gating in KcsA and KvAP. Analysis of the molecular identity of the pH sensor in the prokaryotic potassium channel KcsA identified several key mutants that stabilized the KcsA inner bundle gate in the fully open conformation at neutral pH, a fact that makes possible the crystallographic analyses of KcsA in a variety of functional states. Additional mutations in the selectivity filter were designed towards the determination of a fully conductive and an inactivated form of the channel and the probing of modal gating events.