ASD v2.0: updated content and novel features focusing on allosteric regulation

作者：Huang, Zhimin; Mou, Linkai; Shen, Qiancheng; Lu, Shaoyong; Li, Chuangang; Liu, Xinyi; Wang, Guanqiao; Li, Shuai; Geng, Lv; Liu, Yaqin; Wu, Jiawei; Chen, Guoqiang; Zhang, Jian^*

来源：Nucleic Acids Research, 2014, 42(D1): D510-D516.

DOI：10.1093/nar/gkt1247

• CRYSTAL-STRUCTURE
• T-STATE
• BINDING
• MODULATION
• DATABASE
• SITES
• TRANSITIONS
• PROTEINS
• RESOURCE
• SEQUENCE

Allostery is the most direct and efficient way for regulation of biological macromolecule function and is induced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. AlloSteric Database (ASD, http://mdl.shsmu.edu.cn/ASD) has been developed to provide comprehensive information on allostery. Owing to the inherent high receptor selectivity and lower target-based toxicity, allosteric regulation is expected to assume a more prominent role in drug discovery and bioengineering, leading to the rapid growth of allosteric findings. In this updated version, ASD v2.0 has expanded to 1286 allosteric proteins, 565 allosteric diseases and 22 008 allosteric modulators. A total of 907 allosteric site-modulator structural complexes and >200 structural pairs of orthosteric/allosteric sites in the allosteric proteins were constructed for researchers to develop allosteric site and pathway tools in response to community demands. Up-to-date allosteric pathways were manually curated in the updated version. In addition, both the front-end and the back-end of ASD have been redesigned and enhanced to allow more efficient access. Taken together, these updates are useful for facilitating the investigation of allosteric mechanisms, allosteric target identification and allosteric drug discovery.

• 出版日期2014-1
• 单位上海大学; 大连医科大学; 上海交通大学