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Disordered proteins:
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Protein disorder:
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Default Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-

Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase.

Related Articles Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase.

Biochemistry. 2004 Mar 30;43(12):3404-14

Authors: Saraswat V, Azurmendi HF, Mildvan AS


The solution structure of the ternary MutT enzyme-Mg(2+)-8-oxo-dGMP complex showed the proximity of Asn119 and Arg78 and the modified purine ring of 8-oxo-dGMP, suggesting specific roles for these residues in the tight and selective binding of this nucleotide product [Massiah, M. A., Saraswat, V., Azurmendi, H. F., and Mildvan, A. S. (2003) Biochemistry 42, 10140-10154]. These roles are here tested by mutagenesis. The N119A, N119D, R78K, and R78A single mutations and the R78K/N119A double mutant showed very small effects on k(cat) (
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