| 초록 |
Aquaporin-0(AQP0) acts as not only water pore but also the 11-13 nm ‘thin lens junction’ that assembles after proteolytic cleavage of the cytoplasmic termini. Recently, the structure of the AQP0-mediated membrane junction determined by electron microscopy shows the closed water pore where it contains three water molecules while seven water molecules are found inside the open pore of the nonjuctional-AQP0. From the results, it has been suggested that the loop located on the extracellular side is rearranged due to the proteolytic cleavage of the cytoplasmic termini, and that the resulting conformation of pro38 residue at the center of AQP0 tetramers becomes the rosette-like structure that mediate the major junctional contact. In this work, we generate a model structure for the closed water pore of AQP0 using atomistic molecular simulations, and the resulting structure is investigated to clarify the reason why the conformational changes of the loop occurs at the extracellular side. |
