新的α/β水解酶W14和W15的三维结构模建及分子对接研究

Homology Modeling and Docking Studies of Novel α/β Hydrolase Fold Proteins W14 and W15

利用同源模建和分子动力学模拟方法,模建了两个新发现的α/β水解酶超家族成员W14和W15的三维结构,并通过与α-醋酸萘酯的对接研究,从理论上提出Gly82和Val13为形成"氧洞"的关键残基,有利于稳定水解过程中的带负电的过渡态,以及其它对复合物形成起到重要作用的氨基酸残基.

Three dimensional structure of novel α/β hydrolase fold proteins W14 and W15 were modeled by using homology and molecular dynamics methods. On the basis of the modeling, the components and the structures of active sites in W14 and W15 were analyzed and compared. The docking of 1-naphtyl acetate with the two proteins was also performed and compared. Gly82 and Vail3 were key residues to form the oxyanion-hole and stabilized the negatively charged transition state that occurs during hydrolysis. Other important residues for binding were also identified.