Key result
Human ISG20 crystal structure at 1.9 A resolution reveals distinctive residues explaining RNA substrate preference.
Population
Human ISG20 complexed with two Mn2+ ions and uridine 5'-monophosphate (UMP)
Design
Preclinical
Authors
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Elucidates ISG20 mechanism; leaves open validation and therapeutic targeting in immunity or cardiovascular disease.
The crystal structure of human ISG20 reveals its catalytic mechanism and structural basis for RNA substrate preference.
Horio et al. (2004) studied this question. ISG20 was evaluated on Crystal structure. The crystal structure of human ISG20 complexed with Mn2+ and UMP was solved at 1.9 A resolution, revealing distinctive residues Met14 and Arg53 that may explain its preference for RNA substrates.
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