Poly (ADP-ribose) polymerase

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Template:STRUCTURE 3l3l

Function

Poly (ADP-ribose) polymerase (PARP) is involved in DNA repair and programmed cell death. The PARP family contains 17 members. PARP is composed of 4 domains. Among them are the N terminal DNA-binding domain which contains 2 zinc fingers; auto modification domain which contains a WGR-rich domain; C terminal which includes the catalytic domain (or PARP domain).

• PARP-1 and PARP-2 recognize and is activated by DNA breaks^[1], ^[2].
  
• PARP-3 prevents from extensive end resection to promote double-strand DNA repair ^[3].
  
• PARP-10 contains a RNA recognition motif (RRM).
  
• Tankyrase (Tank) is a PARP which contains ankyrin repeats (a 33-residue repeat with 2 α-helices separated by loops).

3D Structures of Poly (ADP-ribose) polymerase

Updated on 05-July-2016

References

1. ↑ Shall S, de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model? Mutat Res. 2000 Jun 30;460(1):1-15. PMID:10856830
2. ↑ Dantzer F, Giraud-Panis MJ, Jaco I, Ame JC, Schultz I, Blasco M, Koering CE, Gilson E, Menissier-de Murcia J, de Murcia G, Schreiber V. Functional interaction between poly(ADP-Ribose) polymerase 2 (PARP-2) and TRF2: PARP activity negatively regulates TRF2. Mol Cell Biol. 2004 Feb;24(4):1595-607. PMID:14749375
3. ↑ Beck C, Robert I, Reina-San-Martin B, Schreiber V, Dantzer F. Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3. Exp Cell Res. 2014 Nov 15;329(1):18-25. doi: 10.1016/j.yexcr.2014.07.003. Epub, 2014 Jul 10. PMID:25017100 doi:http://dx.doi.org/10.1016/j.yexcr.2014.07.003