期刊
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
卷 364, 期 1514, 页码 239-245出版社
ROYAL SOC
DOI: 10.1098/rstb.2008.0125
关键词
ATP-binding cassette (ABC) transporter; crystal structure; membrane transport proteins; mechanism; structure-function relationship
类别
资金
- Swiss National Science Foundation (SNSF)
- Roche Research Fund (RRF)
- National Center for Excellence in Research (NCCR) Structural Biology, Zurich
- Swiss Cancer League Oncosuisse
ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These structures suggest a mechanism by which binding and hydrolysis of ATP by the cytoplasmic, nucleotide-binding domains control the conformation of the transmembrane domains and therefore which side of the membrane the translocation pathway is exposed to. A basic, conserved two-state mechanism can explain active transport of both ABC importers and ABC exporters, but various questions remain unresolved. In this article, I will review some of the crystal structures and the mechanistic insight gained from them. Future challenges for a better understanding of the mechanism of ABC transporters will be outlined.
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