Effect of phosphorylation on the structure and fold of transactivation domain of p53
S Kar, K Sakaguchi, Y Shimohigashi… - Journal of biological …, 2002 - ASBMB
Several phosphorylations are known to occur in the N-terminal transactivation domain of
human p53. To explore the structural effects of these phosphorylations, we have chemically
synthesized the unphosphorylated p53-(1–39) and its three phosphorylated analogs,
phosphorylated at Ser-15, Thr-18, and Ser-20. p53-(1–39) and its Ser-15 and Thr-18
phosphorylated analogs were tested for interaction with p300. The order of binding affinities
was similar to that derived from biochemical experiments with the whole protein, indicating …
human p53. To explore the structural effects of these phosphorylations, we have chemically
synthesized the unphosphorylated p53-(1–39) and its three phosphorylated analogs,
phosphorylated at Ser-15, Thr-18, and Ser-20. p53-(1–39) and its Ser-15 and Thr-18
phosphorylated analogs were tested for interaction with p300. The order of binding affinities
was similar to that derived from biochemical experiments with the whole protein, indicating …