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Publication Abstract from PubMed

BACKGROUND: Drosha is a nuclear RNase III enzyme that initiates processing of regulatory microRNA. Together with partner protein DiGeorge syndrome critical region 8 (DGCR8), it forms the Microprocessor complex, which cleaves precursor transcripts called primary microRNA to produce hairpin precursor microRNA. In addition to two RNase III catalytic domains, Drosha contains a C-terminal double-stranded RNA-binding domain (dsRBD). To gain insight into the function of this domain, we determined the nuclear magnetic resonance (NMR) solution structure. RESULTS: We report here the solution structure of the dsRBD from Drosha (Drosha-dsRBD). The alphabetabetabetaalpha fold is similar to other dsRBD structures. A unique extended loop distinguishes this domain from other dsRBDs of known structure. CONCLUSIONS: Despite uncertainties about RNA-binding properties of the Drosha-dsRBD, its structure suggests it retains RNA-binding features. We propose that this domain may contribute to substrate recognition in the Drosha-DGCR8 Microprocessor complex.

Solution structure of the Drosha double-stranded RNA-binding domain.,Mueller GA, Miller MT, Derose EF, Ghosh M, London RE, Hall TM Silence. 2010 Jan 12;1(1):2. PMID:20226070^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.