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Related Experiment Videos

Apramycin recognition by the human ribosomal decoding site.

Thomas Hermann1, Valentina Tereshko, Eugene Skripkin

  • 1Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, CA 92093, USA. tch@ucsd.edu

Blood Cells, Molecules & Diseases
|January 30, 2007
PubMed
Summary
This summary is machine-generated.

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Apramycin antibiotic binds to human RNA decoding sites, distinct from its bacterial action. This structural insight reveals how apramycin functions differently in eukaryotes and bacteria.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Pharmacology

Background:

  • Aminoglycoside antibiotics target bacterial ribosomal RNA, inhibiting translation fidelity.
  • Apramycin uniquely blocks translocation and binds eukaryotic decoding sites, despite sequence differences.

Purpose of the Study:

  • To determine the crystal structure of human decoding-site RNA complexed with apramycin.
  • To elucidate the molecular recognition mechanism of apramycin at the eukaryotic decoding site.

Main Methods:

  • X-ray crystallography at 1.5 Å resolution.
  • Oligoribonucleotide synthesis of human decoding-site RNA.

Main Results:

  • The crystal structure reveals apramycin binding in the deep groove of the RNA helix.

Related Experiment Videos

  • The human RNA target forms non-canonical base pairs (C.A, G.A) and includes a bulged-out adenine.
  • Apramycin's binding mode at the human site differs significantly from its bacterial target interaction.

    • Conclusions:

    • The distinct binding mode provides a molecular basis for apramycin's differential action in eukaryotes and bacteria.
    • Understanding apramycin's eukaryotic interaction is crucial for its therapeutic potential and off-target effects.