PARP Structure
PARP is composed of four domains of interest: a DNA-binding domain, a caspase-cleaved domain(see below), an auto-modification domain, and a catalytic domain. The DNA-binding domain is composed of two zinc finger motifs. In the presence of damaged DNA (base pair-excised), the DNA-binding domain will bind the DNA and induce a conformational shift. It has been shown that this binding occurs independent of the other domains. This is integral in a programmed cell death model based on caspase cleavage inhibition of PARP. The auto-modification domain is responsible for releasing the protein from the DNA after catalysis. Also, it plays an integral role in cleavage-induced inactivation.
Read more about this topic: Poly ADP Ribose Polymerase
Famous quotes containing the word structure:
“What is the structure of government that will best guard against the precipitate counsels and factious combinations for unjust purposes, without a sacrifice of the fundamental principle of republicanism?”
—James Madison (1751–1836)