Literature DB >> 14706823

Inhibitor-induced structural change of the active site of human poly(ADP-ribose) polymerase.

Takayoshi Kinoshita1, Isao Nakanishi, Masaichi Warizaya, Akinori Iwashita, Yoshiyuki Kido, Kouji Hattori, Takashi Fujii.   

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.

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Year:  2004        PMID： 14706823     DOI： 10.1016/s0014-5793(03)01362-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  24 in total

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