Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex.

ABSTRACT: The homotetrameric tumor suppressor p53 consists of folded core and tetramerization domains, linked and flanked by intrinsically disordered segments that impede structure analysis by x-ray crystallography and NMR. Here, we solved the quaternary structure of human p53 in solution by a combination of small-angle x-ray scattering, which defined its shape, and NMR, which identified the core domain interfaces and showed that the folded domains had the same structure in the intact protein as in fragments. We combined the solution data with electron microscopy on immobilized samples that provided medium resolution 3D maps. Ab initio and rigid body modeling of scattering data revealed an elongated cross-shaped structure with a pair of loosely coupled core domain dimers at the ends, which are acces

SUBMITTER: Tidow H 

PROVIDER: S-EPMC1941468 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature