Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.

Abstract

The crystal structures of the catalytic frag-

The Paralogous GenesRADICAL-INDUCED CELL DEATH1andSIMILAR TO RCD ONE1Have Partially Redundant Functions during Arabidopsis Development

“…Depending on the specific PARP involved, one to hundreds of ADP-Rib units can be attached to the target (Kim et al, 2005). PARPs are found in all groups of eukaryotes and are characterized by the catalytic site, a b-a-loop-B-a NAD + fold, also called the PARP signature (Ruf et al, 1996;Oliver et al, 2004). This family has been best characterized in humans, where there are 18 family members with diverse functional domains outside of the PARP signature Schreiber et al, 2006;Hassa and Hottiger, 2008).…”

PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

“…This homology was rather poor at the amino-acid level. However, three-dimensional modeling revealed that the C-terminal region of PARP-10 folded into a domain similar to the PARP domain of ck-PARP-1 (Ruf et al, 1996) (Figure 3). Together with the demonstration that PARP-10 has PARP activity, this protein represents a previously unknown member of poly(ADP-ribose) polymerases.…”

“…We observed that the human PARP-10 sequence is compatible with the architecture of a PARP domain and the three-dimensional structure of the catalytic domain of PARP-10 was modeled according to this alignment using the coordinates of ck-PARP-1 as template (Ruf et al, 1996) (Figure 3e). Several amino acids in the active center are conserved.…”

“…Models are generated for all chains in a fold library and ranked by the corresponding z-scores (Sippl, 1993). The X-ray structure of the ch-PARP domain (pdb accession code: 1pax) served as a template for the three-dimensional model of the catalytic domain of PARP-10 ( Ruf et al, 1996). Based on the alignment generated by the fold recognition procedure, aminoacid residues were exchanged in the template.…”

Novel Mutations of the PARP-1 Gene Associated with Colorectal Cancer in the Saudi Population

“…This motif is found in the carboxylic-terminal of AMD of only three human PARP-like proteins: PARP-1, PARP-2, and PARP-3 (Hassa et al, 2006;Krishnakumar and Kraus, 2010). The third domain is the carboxylterminal catalytic domain (CD) that catalyzes three different enzymatic reactions: the attachment of the first ADP-ribose moiety onto an acceptor amino acid (initiation reaction), the addition of further ADP-ribose units onto already existing ones (elongation reaction), and the generation of branching points (branching reaction) (Ruf et al, 1996). It is composed of a PARP signature motif; a highly evolutionally conservative sequence that contains key amino acid residues involve in the formation of both the active site and NAD + acceptor site (Rouleau et al, 2010).…”