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Novel destabilization of nucleotide binding by the gamma phosphate of ATP in the yeast SR protein kinase Sky1p.
Aubol BE, Nolen B, Shaffer J, Ghosh G, Adams JA. Aubol BE, et al. Biochemistry. 2003 Nov 11;42(44):12813-20. doi: 10.1021/bi035200c. Biochemistry. 2003. PMID: 14596595
The yeast SRPK, Sky1p, rapidly phosphorylates its natural substrate Npl3 but binds ATP with a high K(m), suggesting that some of these distinctive structural features may be correlated with nucleotide binding [Aubol et al. (2002) Biochemistry 41, 10002-10009]. ...Th …
The yeast SRPK, Sky1p, rapidly phosphorylates its natural substrate Npl3 but binds ATP with a high K(m), suggesting that some of these disti …
33 results