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Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.(REPORTS)(Author abstract)(Report)

Langelier, Marie - France ; Planck, Jamie L. ; Roy, Swati ; Pascal, John M.

Science, May 11, 2012, Vol.336(6082), p.728(5) [Tạp chí có phản biện]

ISSN: 0036-8075

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  • Nhan đề:
    Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.(REPORTS)(Author abstract)(Report)
  • Tác giả: Langelier, Marie - France ; Planck, Jamie L. ; Roy, Swati ; Pascal, John M.
  • Chủ đề: Adenosine Diphosphate -- Reports ; Protein Conformation -- Research ; Dna Damage -- Research
  • Là 1 phần của: Science, May 11, 2012, Vol.336(6082), p.728(5)
  • Mô tả: Poly(ADP-ribose) polymerase-1 (PARP-1) (ADP, adenosine diphosphate) has a modular domain architecture that couples DNA damage detection to poly(ADP-ribosyl)ation activity through a poorly understood mechanism. Here, we report the crystal structure of a DNA double-strand break in complex with human PARP-1 domains essential for activation (Zn1, Zn3, WGR-CAT). PARP-1 engages DNA as a monomer, and the interaction with DNA damage organizes PARP-1 domains into a collapsed conformation that can explain the strong preference for automodification. The Zn1, Zn3, and WGR domains collectively bind to DNA, forming a network of interdomain contacts that links the DNA damage interface to the catalytic domain (CAT). The DNA damage--induced conformation of PARP-1 results in structural distortions that destabilize the CAT. Our results suggest that an increase in CAT protein dynamics underlies the DNA-dependent activation mechanism of PARP-1. 10.1126/science.1216338
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0036-8075

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