Schmitt Lutz, Tampé Robert
Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie Strasse 9, Germany.
Curr Opin Struct Biol. 2002 Dec;12(6):754-60. doi: 10.1016/s0959-440x(02)00399-8.
ATP-binding cassette (ABC) transporters are central to many physiological processes, including the uptake of nutrients, the non-classical secretion of signaling molecules and toxins, multidrug resistance and the development of human disease. As one might expect from this spectrum of translocation events, these ubiquitous, ATP-dependent pumps or channels are capable of transporting an enormous variety of substrates, ranging from small ions to large proteins. Recently determined structures of full-length ABC transporters and isolated ABC domains have increased our understanding of the functional mechanism of these proteins.
ATP结合盒(ABC)转运蛋白在许多生理过程中起着核心作用,包括营养物质的摄取、信号分子和毒素的非经典分泌、多药耐药性以及人类疾病的发展。从这种转运事件的范围可以预期,这些普遍存在的、依赖ATP的泵或通道能够转运各种各样的底物,从小离子到大蛋白质。最近确定的全长ABC转运蛋白和分离的ABC结构域的结构,增加了我们对这些蛋白质功能机制的理解。