Key result
Base pairing and tertiary interactions between SL1-SL2 domains contribute a large free energy increment of -10 kcal/mol, acting as the primary determinant for retroviral RNA dimer stability.
Population
Moloney murine sarcoma gamma retrovirus RNA dimerization domain sequence variants
Design
Preclinical
Authors
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May guide antiviral design against retroviral packaging; leaves open in vivo efficacy and clinical translation.
The SL1-SL2 domain is the primary determinant of stability for the gamma retroviral genomic RNA dimer, contributing significantly more free energy than PAL1 and PAL2 duplexes.
Gherghe et al. (2006) studied Retroviral genomic RNA dimerization. SL1-SL2 domain interactions vs. PAL1 and PAL2 intermolecular duplexes was evaluated on Free energy increment (stability). Base pairing and tertiary interactions between SL1-SL2 domains contribute a large free energy increment of -10 kcal/mol, acting as the primary determinant for retroviral RNA dimer stability.
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