Article
Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of beta-actin.
European journal of biochemistry - 1 Oct 1999
Schüler H, Korenbaum E, Schutt C E, Lindberg U, Karlsson R
Abstract excerpt
This paper compares wild-type and two mutant beta-actins, one in which Ser14 was replaced by a cysteine, and a second in which both Ser14 and Asp157 were exchanged (Ser14-->Cys and Ser14-->Cys, Asp157-->Ala, respectively). Both of these residues are part of invariant sequences in the loops, which bind the ATP phosphates, in the interdomain cleft of actin. The increased nucleotide exchange rate, and the decreased...
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