Publication Abstract from PubMed
The crystal structure of human recombinant poly(ADP-ribose) polymerase (PARP) complexed with a potent inhibitor, FR257517, was solved at 3.0 A resolution. The fluorophenyl part of the inhibitor induces an amazing conformational change in the active site of PARP by motion of the side chain of the amino acid, Arg878, which forms the bottom of the active site. Consequently, a corn-shaped hydrophobic subsite, which consists of the side chains of Leu769, Ile879, Pro881, and the methylene chain of Arg878, newly emerges from the well-known active site.
Inhibitor-induced structural change of the active site of human poly(ADP-ribose) polymerase.,Kinoshita T, Nakanishi I, Warizaya M, Iwashita A, Kido Y, Hattori K, Fujii T FEBS Lett. 2004 Jan 2;556(1-3):43-6. PMID:14706823[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
