Journal
FEBS LETTERS
Volume 556, Issue 1-3, Pages 43-46Publisher
WILEY
DOI: 10.1016/S0014-5793(03)01362-0
Keywords
poly(ADP-ribose) polymerase; inhibitor induced; crystal structure; synchrotron radiation; molecular-molecular interaction; structural change
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The crystal structure of human recombinant poly(ADP-ribose) polymerase (PARP) complexed with a potent inhibitor, FR257517, was solved at 3.0 Angstrom 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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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