2rf5
From Proteopedia
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'''Crystal structure of human tankyrase 1- catalytic PARP domain''' | '''Crystal structure of human tankyrase 1- catalytic PARP domain''' | ||
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| + | ==Overview== | ||
| + | Tankyrases are recently discovered proteins implicated in many important functions in the cell including telomere homeostasis and mitosis. Tankyrase modulates the activity of target proteins through poly(ADP-ribosyl)ation, and here we report the structure of the catalytic poly(ADP-ribose) polymerase (PARP) domain of human tankyrase 1. This is the first structure of a PARP domain from the tankyrase subfamily. The present structure reveals that tankyrases contain a short zinc-binding motif, which has not been predicted. Tankyrase activity contributes to telomere elongation observed in various cancer cells and tankyrase inhibition has been suggested as a potential route for cancer therapy. In comparison with other PARPs, significant structural differences are observed in the regions lining the substrate-binding site of tankyrase 1. These findings will be of great value to facilitate structure-based design of selective PARP inhibitors, in general, and tankyrase inhibitors, in particular. | ||
==About this Structure== | ==About this Structure== | ||
2RF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RF5 OCA]. | 2RF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RF5 OCA]. | ||
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| + | ==Reference== | ||
| + | Zinc binding catalytic domain of human tankyrase 1., Lehtio L, Collins R, van den Berg S, Johansson A, Dahlgren LG, Hammarstrom M, Helleday T, Holmberg-Schiavone L, Karlberg T, Weigelt J, J Mol Biol. 2008 May 23;379(1):136-45. Epub 2008 Apr 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18436240 18436240] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Translocation]] | [[Category: Translocation]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:59:12 2008'' |
Revision as of 06:59, 4 June 2008
Crystal structure of human tankyrase 1- catalytic PARP domain
Overview
Tankyrases are recently discovered proteins implicated in many important functions in the cell including telomere homeostasis and mitosis. Tankyrase modulates the activity of target proteins through poly(ADP-ribosyl)ation, and here we report the structure of the catalytic poly(ADP-ribose) polymerase (PARP) domain of human tankyrase 1. This is the first structure of a PARP domain from the tankyrase subfamily. The present structure reveals that tankyrases contain a short zinc-binding motif, which has not been predicted. Tankyrase activity contributes to telomere elongation observed in various cancer cells and tankyrase inhibition has been suggested as a potential route for cancer therapy. In comparison with other PARPs, significant structural differences are observed in the regions lining the substrate-binding site of tankyrase 1. These findings will be of great value to facilitate structure-based design of selective PARP inhibitors, in general, and tankyrase inhibitors, in particular.
About this Structure
2RF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Zinc binding catalytic domain of human tankyrase 1., Lehtio L, Collins R, van den Berg S, Johansson A, Dahlgren LG, Hammarstrom M, Helleday T, Holmberg-Schiavone L, Karlberg T, Weigelt J, J Mol Biol. 2008 May 23;379(1):136-45. Epub 2008 Apr 3. PMID:18436240 Page seeded by OCA on Wed Jun 4 09:59:12 2008
Categories: Homo sapiens | Single protein | Arrowsmith, C H. | Berg, S van den. | Berglund, H. | Busam, R. | Collins, R. | Dahlgren, L G. | Edwards, A M. | Flodin, S. | Flores, A. | Graslund, S. | Hammarstrom, M. | Herman, M D. | Holmberg-Schiavone, L. | Johansson, I. | Kallas, A. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nordlund, P. | Nyman, T. | Persson, C. | SGC, Structural Genomics Consortium. | Sagemark, J. | Sundstrom, M. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Adp-ribosylation | Alternative splicing | Ank repeat | Catalytic fragment | Chromosomal protein | Crystal structure | Cytoplasm | Glycosyltransferase | Golgi apparatus | Membrane | Mrna transport | Nad | Nuclear pore complex | Nucleus | Parp | Phosphorylation | Protein transport | Sgc | Structural genomic | Structural genomics consortium | Telomere | Transferase | Translocation | Transport
