Key result
X-ray crystallography of the RNA-dependent RNA polymerase from the rabbit hemorrhagic disease virus revealed active and inactive conformations differing by an 8-degree rotation of the thumb domain.
Population
RNA-dependent RNA polymerase (RdRP) from the rabbit hemorrhagic disease virus
Design
Preclinical
Authors
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Structural insights into RHDV RdRP remain preclinical; leaves open extension to human pathogens or antiviral strategies.
The crystal structure of rabbit hemorrhagic disease virus RdRP reveals active and inactive conformations, providing insights into the structure-function relationships of viral polymerases.
Ng et al. (2002) studied Rabbit hemorrhagic disease virus. X-ray crystallography of the RNA-dependent RNA polymerase from the rabbit hemorrhagic disease virus revealed active and inactive conformations differing by an 8-degree rotation of the thumb domain.
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