Tankyrase-2 与强效 Wnt 信号抑制剂相互作用的结构基础。
Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor.
机构信息
Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
出版信息
J Med Chem. 2010 Jul 22;53(14):5352-5. doi: 10.1021/jm100249w.
PMID:20565110
Abstract
We report two crystal structures of the PARP domain of human tankyrase-2 (TNKS2). Tankyrases are involved in fundamental cellular processes such as telomere homeostasis and Wnt signaling. The complex of TNKS2 with the potent inhibitor XAV939 provides insights into the molecular basis of the strong interaction and suggests routes for further development of tankyrase inhibitors.
摘要
我们报告了人端锚聚合酶 2（TNKS2）的 PARP 结构域的两个晶体结构。端锚聚合酶参与基本的细胞过程，如端粒稳态和 Wnt 信号传导。TNKS2 与强效抑制剂 XAV939 的复合物提供了对强相互作用的分子基础的深入了解，并为进一步开发端锚聚合酶抑制剂提供了途径。
Zotero 插件