| Co-Investigator(Kenkyū-buntansha) |
SATO Chikara National Institute of Advanced Industrial Science and Technology, Structure Physiology Group, Chief Scientist, 構造生理研究グループ, 主任研究員
DOI Tomoko JEOL. Ltd., Basic Research department, Chief Scientist, 基礎研究部, 主任研究員
MIYAZAWA Atsuo Kyoto University, RIKEN Harima Institute, Bio-multisome Research Team, Team Leader, 生体マルチソーム研究チーム, 連携研究員 (60247252)
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| Research Abstract |
The following research results were achieved in three years by support of Glant-in Aid for Specially promoted Research from 2001. 1)Structure of water channel, AQP4, was analyzed by over expression technique of Sf9 cells as well as electron crystallography. Based on the structure we could elucidate mechanisms of orthogonal array formation and cell adhesion of the water channel molecules. 2)Structure and gating mechanism of the acetylcholine receptor pore were analyzed by cryo-electron microscopy (J.Mol.Biol., 319, 1165-1176 (2002), Nature, 423, 949-955 (2003)). 3)A new computer program for automatic particle pickup method of single particle analysis, by which structure of voltage-sensitive sodium channel was analyzed (Nature, 409, 1047-1051 (2001)), was developed (J.Struct.Biol., 136, 227-238 (2001)) and enabled us to analyze structure of IP_3 receptor (J.Mol.Biol., 336, 155-164 (2004)). 4)Structure of Homer was analyzed by X-ray crystallography (J.Mol.Biol., 318, 1117-1126 (2002)), and we developed a new Co-localization Expression Technique (Co-LET) for purification of membrane proteins without detergents (BBRC, 295, 756-765 (2002)). 5)We studied interaction of endothelin B receptor with caveoline-1 (Eur.J.Biochem., 270, 1816-1827 (2003)). Structure of rhodopsin was analyzed at 2.6 Å (Proc.Natl.Acad.Sci.USA, 99, 5982-5987 (2002)). The mutations of three residues in connexin26 were studied to obtain the structural insights of the molecule (J.Boil.Chem., 278, 1807-1816 (2003)). The importance of the second PDZ domain for clustering of PSD-95 was revealed (J.Biol.Chem., 277, 3640-3646 (2002)).
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