Crystal structure of human DGCR8 core
Copyright policy )Crystal structure of human DGCR8 core
A complex of Drosha with DGCR8 (or its homolog Pasha) cleaves primary microRNA (pri-miRNA) substrates into precursor miRNA and initiates the microRNA maturation process. Drosha provides the catalytic site for this cleavage, whereas DGCR8 or Pasha provides a frame for anchoring substrate pri-miRNAs. To clarify the molecular basis underlying recognition of pri-miRNA by DGCR8 and Pasha, we determined the crystal structure of the human DGCR8 core (DGCR8S, residues 493-720). In the structure, the two double-stranded RNA-binding domains (dsRBDs) are arranged with pseudo two-fold symmetry and are tightly packed against the C-terminal helix. The H2 helix in each dsRBD is important for recognition of pri-miRNA substrates. This structure, together with fluorescent resonance energy transfer and mutational analyses, suggests that the DGCR8 core recognizes pri-miRNA in two possible orientations. We propose a model for DGCR8's recognition of pri-miRNA.
- Seoul National University Korea (Republic of)
- Pohang University of Science and Technology Korea (Republic of)
Models, Molecular, ENZYME COMPLEX, Protein Conformation, PROTEIN, Proteins, RNA-Binding Proteins, Electrophoretic Mobility Shift Assay, MICROPROCESSOR COMPLEX, Crystallography, X-Ray, NUCLEAR EXPORT, PRIMARY MICRORNAS, MicroRNAs, MOLECULAR-BASIS, C-ELEGANS, Fluorescence Resonance Energy Transfer, DIGEORGE-SYNDROME, Humans, RNA-BINDING DOMAIN, DROSHA-DGCR8 COMPLEX, Protein Binding
Models, Molecular, ENZYME COMPLEX, Protein Conformation, PROTEIN, Proteins, RNA-Binding Proteins, Electrophoretic Mobility Shift Assay, MICROPROCESSOR COMPLEX, Crystallography, X-Ray, NUCLEAR EXPORT, PRIMARY MICRORNAS, MicroRNAs, MOLECULAR-BASIS, C-ELEGANS, Fluorescence Resonance Energy Transfer, DIGEORGE-SYNDROME, Humans, RNA-BINDING DOMAIN, DROSHA-DGCR8 COMPLEX, Protein Binding
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