STRUCTURE DETERMINATION OF KEF CHANNEL CYTOPLASMIC DOMAIN COMPLEX

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 KTN/RCK结构域调节多种钾转运系统和离子通道的跨膜通量。许多争论围绕着调控机制，有不同的模型提出，要么是构成的，构象灵活的结构域八聚体环，要么是四聚态和二聚态之间的化学计量重排，调节离子通量。为了解决这个问题，我们正在从Kef K通道系统中确定KTN结构域的结构，并与其KefF辅助亚单位形成复合体。另外，KefF与FMN结合，而KefC KTN结构域与NAD(H)结合，它们共同形成能够催化新的氧化还原化学的酶活性络合物。因此，这项研究还将提高我们对跨膜离子电导和细胞生物化学如何联系起来创建更高阶现象(如记忆)的理解。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. KTN/RCK domains regulate the transmembrane flux of a variety of K+ transport systems and ion channels. Much controversy surrounds the mechanism of regulation, with alternative models proposing either, a constitutive, conformationally-flexible octameric ring of domains, or stoichiometric rearrangements between tetrameric and dimeric states, modulating ion flux. We are determining the structure of the KTN domain from the Kef K+ channel system, in complex with its KefF ancillary subunit to resolve this issue. Of additional interest, KefF binds FMN while the KefC KTN domain binds NAD(H), and together they form an enzymatically active complex capable of catalyzing novel redox chemistry. Thus, this study will also improve our understanding of how transmembrane ion conductance and cellular biochemistry can be linked to create higher order phenomena such as memory.