2rf5: Difference between revisions

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'''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 [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].

==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: Single protein]]

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[[Category: Translocation]]

[[Category: Transport]]

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@@ Line 11: / Line 11: @@
 '''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==
 RF5 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].
+==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: Single protein]]
@@ Line 69: / Line 75: @@
 [[Category: Translocation]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:47:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 09:59:12 2008''