Walz Thomas, Fujiyoshi Yoshinori, Engel Andreas
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Handb Exp Pharmacol. 2009(190):31-56. doi: 10.1007/978-3-540-79885-9_2.
Progress in the structure determination of AQPs has led to a deep understanding of water and solute permeation by these small integral membrane proteins. The atomic structures now available have allowed the water permeation and exclusion of protons to be monitored by molecular dynamics simulations, and have provided a framework for assessing the water and solute permeation in great detail by site-directed mutations. In spite of this, further structural and molecular dynamics analyses are required to elucidate the basis for regulation as well as for gas permeation, processes that are still to be deciphered.
水通道蛋白结构测定方面的进展使人们对这些小型整合膜蛋白介导的水和溶质渗透有了深入了解。目前已获得的原子结构使得通过分子动力学模拟监测水的渗透和质子的排斥成为可能，并且为通过定点突变详细评估水和溶质的渗透提供了框架。尽管如此，仍需要进一步的结构和分子动力学分析来阐明调节以及气体渗透的基础，而这些过程仍有待破解。
