期刊
PHYSIOLOGICAL REVIEWS
卷 88, 期 2, 页码 351-387出版社
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/physrev.00058.2006
关键词
-
类别
资金
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL053445] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK055835] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM065447, R56GM065447] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R01-HL-53445] Funding Source: Medline
- NIDDK NIH HHS [R01-DK-55835, R01 DK055835] Funding Source: Medline
- NIGMS NIH HHS [R56 GM065447, R01 GM065447, R01-GM65447] Funding Source: Medline
CLC-0 and cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channels play important roles in Cl- transport across cell membranes. These two proteins belong to, respectively, the CLC and ABC transport protein families whose members encompass both ion channels and transporters. Defective function of members in these two protein families causes various hereditary human diseases. Ion channels and transporters were traditionally viewed as distinct entities in membrane transport physiology, but recent discoveries have blurred the line between these two classes of membrane transport proteins. CLC-0 and CFTR can be considered operationally as ligand-gated channels, though binding of the activating ligands appears to be coupled to an irreversible gating cycle driven by an input of free energy. High-resolution crystallographic structures of bacterial CLC proteins and ABC transporters have led us to a better understanding of the gating properties for CLC and CFTR Cl- channels. Furthermore, the joined force between structural and functional studies of these two protein families has offered a unique opportunity to peek into the evolutionary link between ion channels and transporters. A promising byproduct of this exercise is a deeper mechanistic insight into how different transport proteins work at a fundamental level.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据