Coupling of ATP hydrolysis with channel gating by purified, reconstituted CFTR.
Coupling of ATP hydrolysis with channel gating by purified, reconstituted CFTR.
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通过纯化、重构的 CFTR 将 ATP 水解与通道门控耦合。
DOI：
10.1023/a:1022435007193
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发表时间：
1997
影响因子：
3
通讯作者：
Ramjeesingh,M
中科院分区：
文献类型：
--
作者：
Bear,CE;Li,C;Galley,K;Wang,Y;Garami,E;Ramjeesingh,M
囊性纤维化跨膜传导调节因子（CFTR）是位于上皮细胞顶膜上的氯离子通道。我们最近的研究纯化，重建CFTR显示，它也作为一个ATP酶的功能，可能有ATP水解和通道门控之间的耦合。ATP转换率和通道门控都很慢，在0.2到1 s-1的范围内，并且这两种活性在位于假定的核苷酸结合基序中的致病突变中被抑制。我们未来的研究将使用纯化的蛋白质，以了解水解和通道功能之间的耦合的结构基础和机制。
The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel situated on the apical membrane of epithelial cells. Our recent studies of purified, reconstituted CFTR revealed that it also functions as an ATPase and that there may be coupling between ATP hydrolysis and channel gating. Both the ATP turnover rate and channel gating are slow, in the range of 0.2 to 1 s−1, and both activities are suppressed in a disease-causing mutation situated in a putative nucleotide binding motif. Our future studies using purified protein will be directed toward understanding the structural basis and mechanism for coupling between hydrolysis and channel function.