Rudnick Gary
Department of Pharmacology, Yale University School of Medicine , New Haven, CT , USA.
Mol Membr Biol. 2013 Nov;30(7):355-9. doi: 10.3109/09687688.2013.842658.
Abstract The availability of high-resolution atomic structures for transport proteins provides unprecedented opportunities for understanding their mechanism of action. The details of conformational change can be deduced from these structures, especially when multiple conformations are available. However, the singular ability of transporters to couple the movement of one solute to that of another requires even more information than what is supplied by a crystal structure. This short commentary discusses how recent biochemical and biophysical studies are beginning to reveal how solute coupling is achieved.
摘要 转运蛋白高分辨率原子结构的可得性为理解其作用机制提供了前所未有的机会。构象变化的细节可从这些结构中推导出来,尤其是当有多个构象时。然而,转运蛋白将一种溶质的移动与另一种溶质的移动相偶联的独特能力需要比晶体结构所提供的更多信息。本简短评论讨论了最近的生化和生物物理研究如何开始揭示溶质偶联是如何实现的。