Argonaute MID domain takes centre stage

EMBO Rep. 2010 Aug;11(8):564-5. doi: 10.1038/embor.2010.110. Epub 2010 Jul 16.

Abstract

Two recent papers, one in EMBO reports and one in Nature give us the first eukaryotic structures of Argonaute MID domains; providing a structural basis for the 5′-nucleotide recognition of the guide strand and a possible explanation for the allosteric regulation of RNA binding.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Animals
  • Argonaute Proteins
  • Drosophila Proteins* / chemistry
  • Drosophila Proteins* / genetics
  • Drosophila Proteins* / metabolism
  • Drosophila melanogaster
  • Eukaryotic Initiation Factor-2* / chemistry
  • Eukaryotic Initiation Factor-2* / genetics
  • Eukaryotic Initiation Factor-2* / metabolism
  • Eukaryotic Initiation Factors* / chemistry
  • Eukaryotic Initiation Factors* / genetics
  • Eukaryotic Initiation Factors* / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Gene Silencing*
  • Humans
  • MicroRNAs / genetics
  • MicroRNAs / metabolism
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • AGO1 protein, Drosophila
  • AGO2 protein, human
  • Argonaute Proteins
  • Drosophila Proteins
  • Eukaryotic Initiation Factor-2
  • Eukaryotic Initiation Factors
  • Fungal Proteins
  • MicroRNAs
  • QDE-2 protein, Neurospora crassa