1UK0

Crystal structure of catalytic domain of human poly(ADP-ribose) polymerase with a novel inhibitor

Summary for 1UK0

• Entry DOI: 10.2210/pdb1uk0/pdb
• Related: 1UK1
• Descriptor: Poly [ADP-ribose] polymerase-1, 2-{3-[4-(4-FLUOROPHENYL)-3,6-DIHYDRO-1(2H)-PYRIDINYL]PROPYL}-8-METHYL-4(3H)-QUINAZOLINONE (3 entities in total)
• Functional Keywords: protein-inhibitor complex, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P09874
• Total number of polymer chains: 2
• Total formula weight: 79148.64

Authors

Kinoshita, T. (deposition date: 2003-08-13, release date: 2004-01-27, Last modification date: 2023-12-27)

Primary citation

Kinoshita, T.,Nakanishi, I.,Warizaya, M.,Iwashita, A.,Kido, Y.,Hattori, K.,Fujii, T.
Inhibitor-induced structural change of the active site of human poly(ADP-ribose) polymerase.
Febs Lett., 556:43-46, 2004

PubMed Abstract: 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.

PubMed: 14706823
DOI: 10.1016/S0014-5793(03)01362-0

Experimental method

X-RAY DIFFRACTION (3 Å)