刊名:Biochimica et Biophysica Acta (BBA) - General Subjects
出版年:2017
出版时间:February 2017
年:2017
卷:1861
期:2
页码:168-177
全文大小:1720 K
卷排序:1861
文摘
A homology model of the N-terminal cysteine rich domain of the Smoothened receptor was generated. Molecular dynamics and binding energy calculations of the model in complex with a series of oxysterols were performed. Hh modulatory activity correlated well with predicted binding energy: Hh antagonists were predicted to bind with high energy and Hh agonists were predicted to bind with low energy. These computational studies led to the identification of a new Hh inhibitor with the oxysterol scaffold.