Structural biology of the p53 tumour suppressor.
The p53 tumour suppressor protein has presented a challenge for structural biology for more than two decades. The complete p53 molecule has eluded numerous attempts to determine its structure, presumably owing to the intrinsic conformational flexibility that is essential to the protein's function. Recent data obtained by X-ray crystallography, NMR spectroscopy and electron microscopy provide new insight into the quaternary architecture of the whole molecule and new strategies for examining how these structures correlate with the cell and molecular biology of the 'Guardian of the Genome'.
Okorokov
Andrei L
AL
Wolfson Institute for Biomedical Research, University College London, Gower Street, London, UK.
Orlova
Elena V
EV
D000818:Animals; D001483:Base Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
D010455:Peptides; D016159:Tumor Suppressor Protein p53