Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor.
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.
Karlberg
Tobias
T
Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
Markova
Natalia
N
Johansson
Ida
I
Hammarström
Martin
M
Schütz
Patrick
P
Weigelt
Johan
J
Schüler
Herwig
H
D018360:Crystallography, X-Ray; D006575:Heterocyclic Compounds, 3-Ring / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D015398:Signal Transduction; D038501:Tankyrases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D051153:Wnt Proteins / Q000502:physiology*
D006575:Heterocyclic Compounds, 3-Ring; D011994:Recombinant Proteins; D051153:Wnt Proteins; C544261:XAV939; C437334:TNKS2 protein, human; D038501:Tankyrases