Structural Basis for the Interaction between Tankyrase-2 and a Potent Wnt-Signaling Inhibitor

被引：107

作者：

Karlberg, Tobias ^{[1
]}

Markova, Natalia ^{[1
,2
]}

Johansson, Ida ^{[1
]}

Hammarstrom, Martin ^{[1
]}

Schutz, Patrick ^{[1
]}

Weigelt, Johan ^{[1
]}

Schuler, Herwig ^{[1
]}

机构：

[1] Karolinska Inst, Dept Med Biochem & Biophys, Struct Genom Consortium, S-17177 Stockholm, Sweden

[2] iNovacia AB, S-11251 Stockholm, Sweden

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2010年 / 53卷 / 14期

基金：

加拿大创新基金会; 英国惠康基金;

关键词：

POLY(ADP-RIBOSE) POLYMERASE; CATALYTIC DOMAIN; BINDING; CANCER;

D O I：

10.1021/jm100249w

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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.

引用

页码：5352 / 5355

页数：4

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