Author: Jordan, Paul C; Stevens, Sarah K; Deval, Jerome
Title: Nucleosides for the treatment of respiratory RNA virus infections Document date: 2018_3_21
ID: txaoz7oh_18
Snippet: A recent crystal structure of the MTase domain from HMPV has provided additional clues into this reaction (see Figure 3 ). 72 A 406-residue fragment was expressed, consisting of the CR-IV containing the putative MTase with an additional C-terminal K-K-G motif (termed CR-VIþ). With the exception of the K-K-G motif, the fold of the HMPV MTase domain indicates a conserved fold compared to VSV. 72 While the CR-VIþ was active, the reaction rate was .....
Document: A recent crystal structure of the MTase domain from HMPV has provided additional clues into this reaction (see Figure 3 ). 72 A 406-residue fragment was expressed, consisting of the CR-IV containing the putative MTase with an additional C-terminal K-K-G motif (termed CR-VIþ). With the exception of the K-K-G motif, the fold of the HMPV MTase domain indicates a conserved fold compared to VSV. 72 While the CR-VIþ was active, the reaction rate was very slow and structural and biochemical results did not clearly identify active site residues. This suggests that MTase requires other co-factors or additional parts of the L protein to be catalytic.
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