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Zinc binding catalytic domain of human tankyrase 1.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Lehtiö L,Collins R,van den Berg S,Johansson A,Dahlgren LG,Hammarström M,Helleday T,Holmberg-Schiavone L,Karlberg T,Weigelt J

doi

10.1016/j.jmb.2008.03.058

subject

Has Abstract

pub_date

2008-05-23 00:00:00

pages

136-45

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(08)00389-6

journal_volume

379

pub_type

杂志文章

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