期刊
TRENDS IN PHARMACOLOGICAL SCIENCES
卷 36, 期 11, 页码 724-736出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2015.08.003
关键词
-
资金
- National Institute of General Medical Sciences
- [GM064700]
- [GM094551]
Analysis of binding energy hot spots at protein surfaces can provide crucial insights into the prospects for successful application of fragment-based drug discovery (FBDD), and whether a fragment hit can be advanced into a high-affinity, drug-like ligand. The key factor is the strength of the top ranking hot spot, and how well a given fragment complements it. We show that published data are sufficient to provide a sophisticated and quantitative understanding of how hot spots derive from a protein 3D structure, and how their strength, number, and spatial arrangement govern the potential for a surface site to bind to fragment-sized and larger ligands. This improved understanding provides important guidance for the effective application of FBDD in drug discovery.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据