Key result
The retroviral dimerization domain adopts a compact architecture characterized by close packing of its constituent helices, with partially overlapping flexible domains in monomer and dimer states.
Population
Moloney murine sarcoma virus minimal dimerization active sequence (MiDAS) RNA
Design
Preclinical
Authors
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May inform antiviral design targeting RNA dimerization; leaves open translation to human therapeutics.
The retroviral dimerization domain adopts a compact architecture with close packing of constituent helices, providing insight into the fundamental role of dimeric RNA in retroviral biology.
Badorrek et al. (2006) studied Retroviral genomic RNA dimer structure. Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE) and hydroxyl radical cleavage was evaluated on Secondary structure model and global architecture of the minimal dimerization active sequence (MiDAS). The retroviral dimerization domain adopts a compact architecture characterized by close packing of its constituent helices, with partially overlapping flexible domains in monomer and dimer states.
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