Structural studies of specific intermolecular interactions and self-aggregation of biomolecules and their application to drug design.
Information on the structural basis of intermolecular recognition or self-aggregation of biomolecules at the atomic level is important to understand biological functions and to develop devices for treating disorders caused by abnormal functions. Thus structural analysis of specific intermolecular or intramolecular interactions of biomolecules has been performed using various physicochemical approaches. Herein, the following three subjects are reviewed: (1) structural analyses of mRNA cap structure recognition by eukaryotic initiation factor 4E and its functional regulation by endogenous 4E-binding protein; (2) structural studies of self-aggregation mechanism of microtubule-binding domain in tau protein and aggregation inhibitor; and (3) molecular design of cathepsin B-specific inhibitor.
Ishida
Toshimasa
T
Osaka University of Pharmaceutical Sciences, Nasahara, Takatsuki, Japan. ishida@gly.oups.ac.jp
D015195:Drug Design; D039561:Eukaryotic Initiation Factor-4E / Q000737:chemistry / Q000378:metabolism; D012315:RNA Caps / Q000737:chemistry / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism
D039561:Eukaryotic Initiation Factor-4E; D012315:RNA Caps; D012333:RNA, Messenger