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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2010-7-29
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1520-4804
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
22
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5352-5
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pubmed:meshHeading |
pubmed-meshheading:20565110-Crystallography, X-Ray,
pubmed-meshheading:20565110-Heterocyclic Compounds, 3-Ring,
pubmed-meshheading:20565110-Humans,
pubmed-meshheading:20565110-Models, Molecular,
pubmed-meshheading:20565110-Protein Structure, Tertiary,
pubmed-meshheading:20565110-Recombinant Proteins,
pubmed-meshheading:20565110-Signal Transduction,
pubmed-meshheading:20565110-Tankyrases,
pubmed-meshheading:20565110-Wnt Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor.
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pubmed:affiliation |
Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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