摘要
利用同源模建的方法,构建了DDAH-2的三位结构.并与L-瓜氨酸、L-高半胱氨酸分别进行对接研究.其中,Asp77,Gly269,Glu27和Arg96是与L-瓜氨酸相互作用较强的残基,Asp77,His171,Asp125和Ala270是与L-高半胱氨酸相互作用较强的残基.尤其Asp77是在两种复合物中同时起重要作用的氨基酸,并且它与抑制剂之间都形成了氢键.
Dimethylarginine dimethylaminohydrolase （DDAH） is involved in the regulation of nitric oxide synthase （NOS） .The structure of DDAH might be useful in the therapeutic treatment of NOS dysfunction-diseases .3D structure of DDAH-2 was modeled by using Homology. With the aid of the automated inolecular docking,the inhibition effect of L-citmlline and L-homocysteine for DDAH-2,respectively,were studied.By analyzing the structures of the enzyme in complex with L-citrulline,and L-homocysteine which has the lowest energy among the ten collected conformations,respectively,we know that the residues Asp77, Gly269, Glu27,Arg96 with L-citrulline,and the residues Asp77, His171, Asp125,Ala270 with L-homocysteine play an important role in the binding for the enzyme in complex, respectively. Asp77 is an important residues in beth complex,while it forms hydrogen bond to L-citrulline and L-homocysteine.
出处
《分子科学学报》
CAS
CSCD
北大核心
2009年第2期116-120,共5页
Journal of Molecular Science
基金
黑龙江省自然科学基金资助项目(B200605)
黑龙江省博士后基金资助项目
