Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53

Autor: M G, Mateu, M M, Sánchez Del Pino, A R, Fersht
Rok vydání: 1999
Předmět:
Zdroj: Nature structural biology. 6(2)
ISSN: 1072-8368
Popis: We have analyzed the folding pathway of the tetramerization domain of the tumor suppressor protein p53. Structures of transition states were determined from phi-values for 25 mutations, including leucine to norvaline, and the analysis encompassed nearly every residue in the domain. Denatured monomers fold and dimerize, through a transition state with little native structure, to form a transient, highly structured dimeric intermediate. The intermediate dimerizes, through a native-like transition state with the primary dimers fully folded but with interdimer interactions only partially formed, to form the native tetramer as a 'dimer of dimers'.
Databáze: OpenAIRE