title: Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor.
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.
authors.affiliation: Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
authors.forename: Tobias
authors.initials: T
authors.lastname: Karlberg
authors.forename: Natalia
authors.initials: N
authors.lastname: Markova
authors.forename: Ida
authors.initials: I
authors.lastname: Johansson
authors.forename: Martin
authors.initials: M
authors.lastname: Hammarström
authors.forename: Patrick
authors.initials: P
authors.lastname: Schütz
authors.forename: Johan
authors.initials: J
authors.lastname: Weigelt
authors.forename: Herwig
authors.initials: H
authors.lastname: Schüler
mesh_terms: 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*
chemical_list: D006575:Heterocyclic Compounds, 3-Ring; D011994:Recombinant Proteins; D051153:Wnt Proteins; C544261:XAV939; C437334:TNKS2 protein, human; D038501:Tankyrases