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Structural basis for double-stranded RNA processing by Dicer

Academic Article
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Overview

authors

  • MacRae, Ian
  • Zhou, K. H.
  • Li, F.
  • Repic, A.
  • Brooks, A. N.
  • Cande, W. Z.
  • Adams, P. D.
  • Doudna, J. A.

publication date

  • January 2006

journal

  • Science  Journal

abstract

  • The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.

subject areas

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • Crystallography, X-Ray
  • Giardia lamblia
  • Humans
  • Lanthanoid Series Elements
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • RNA Interference
  • RNA, Double-Stranded
  • RNA, Protozoan
  • Recombinant Fusion Proteins
  • Ribonuclease III
  • Schizosaccharomyces
  • Structure-Activity Relationship
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1121638

PubMed ID

  • 16410517
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Additional Document Info

start page

  • 195

end page

  • 198

volume

  • 311

issue

  • 5758

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