Structural Basis for the Interaction between Tankyrase-2 and a Potent Wnt-Signaling Inhibitor
Structural Basis for the Interaction between Tankyrase-2 and a Potent Wnt-Signaling Inhibitor
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DOI：
10.1021/jm100249w
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发表时间：
2010-07-22
影响因子：
7.3
通讯作者：
Schuler, Herwig
中科院分区：
文献类型：
--
作者：
Karlberg, Tobias;Markova, Natalia;Schuler, Herwig
我们报告了人端锚聚合酶2（TNKS2）的PARP结构域的两种晶体结构。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。TNKS 2与强效抑制剂XAV 939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。
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.