Abstract
Our earlier suggestion that the G245C mutation in p53 generates an additional zinc binding site, overlapping with the normal zinc binding site, has been supported by molecular modeling. The energy of interaction between a zinc ion and the new site in the G245 mutant is comparable to that for the normal site in wild-type p53. The presence of the additional site in the mutant can distort its conformation when it interacts with DNA. Effects of other mutations on the energy of zinc binding to the normal site have been calculated.
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Fomin, E.S., Ivanisenko, V.A. Corroboration of the functional role of the additional zinc binding site in the G245C mutant form of the p53 protein. BIOPHYSICS 51 (Suppl 1), 35–38 (2006). https://doi.org/10.1134/S0006350906070074
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DOI: https://doi.org/10.1134/S0006350906070074