Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region
Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.
This entry represents de N-terminal helical region of PADR1 zinc-binding domain found in poly(ADP-ribose) polymerase-1 (PARP-1) from human and its homologues. The PADR1, known as the third zinc-binding domain (Zn3) localises between the N-terminal PA ...
This entry represents de N-terminal helical region of PADR1 zinc-binding domain found in poly(ADP-ribose) polymerase-1 (PARP-1) from human and its homologues. The PADR1, known as the third zinc-binding domain (Zn3) localises between the N-terminal PARP-type zinc fingers (Zn1 and Zn2) and the central BRCT domain; it is involved in protein-protein interactions that orchestrate PARP-1 activation and are critical to the DNA-dependent stimulation of PARP-1 [1-5].
This is the zinc ribbon fold of the PADR1 domain found in poly(ADP-ribose)-polymerases, referred to as the third zinc-binding domain of these proteins [1-5]. The PADR1 domain is involved in protein-protein interactions that orchestrate PARP-1 activat ...
This is the zinc ribbon fold of the PADR1 domain found in poly(ADP-ribose)-polymerases, referred to as the third zinc-binding domain of these proteins [1-5]. The PADR1 domain is involved in protein-protein interactions that orchestrate PARP-1 activation and are critical to the DNA-dependent stimulation of PARP-1. PADR1 consists of an N-terminal helical region, the central zinc ribbon fold and a C-terminal tail.
Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component ...
Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active [2].
This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The ...
This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.
