胶束中钠钾ATP酶调节蛋白FXYD2b的结构：对膜-水界面精氨酸的影响
Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines.
作者信息
Gong Xiao-Min, Ding Yi, Yu Jinghua, Yao Yong, Marassi Francesca M
机构信息
Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
出版信息
Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):299-306. doi: 10.1016/j.bbamem.2014.04.021. Epub 2014 May 2.
Abstract
FXYD2 is a membrane protein responsible for regulating the function of the Na,K-ATPase in mammalian kidney epithelial cells. Here we report the structure of FXYD2b, one of two splice variants of the protein, determined by NMR spectroscopy in detergent micelles. Solid-state NMR characterization of the protein embedded in phospholipid bilayers indicates that several arginine side chains may be involved in hydrogen bond interactions with the phospholipid polar head groups. The structure and the NMR data suggest that FXYD2b could regulate the Na,K-ATPase by modulating the effective membrane surface electrostatics near the ion binding sites of the pump.
摘要
FXYD2是一种膜蛋白，负责调节哺乳动物肾上皮细胞中钠钾ATP酶的功能。在此，我们报告了该蛋白的两种剪接变体之一FXYD2b的结构，它是通过在去污剂胶束中进行核磁共振光谱测定的。对嵌入磷脂双分子层中的该蛋白进行固态核磁共振表征表明，几个精氨酸侧链可能参与了与磷脂极性头部基团的氢键相互作用。该结构和核磁共振数据表明，FXYD2b可能通过调节泵离子结合位点附近的有效膜表面静电来调节钠钾ATP酶。
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