| Literature DB >> 15566281 |
Craig A Coburn1, Shawn J Stachel, Yue-Ming Li, Diane M Rush, Thomas G Steele, Elizabeth Chen-Dodson, M Katharine Holloway, Min Xu, Qian Huang, Ming-Tain Lai, Jillian DiMuzio, Ming-Chih Crouthamel, Xiao-Ping Shi, Vinod Sardana, Zhongguo Chen, Sanjeev Munshi, Lawrence Kuo, Gergely M Makara, D Allen Annis, Praveen K Tadikonda, Huw M Nash, Joseph P Vacca, Tong Wang.
Abstract
A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors.Entities:
Mesh：
Substances：
Year: 2004 PMID： 15566281 DOI： 10.1021/jm049388p
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446