Okorokov Andrei L, Orlova Elena V
Wolfson Institute for Biomedical Research, University College London, Gower Street, London, UK.
Curr Opin Struct Biol. 2009 Apr;19(2):197-202. doi: 10.1016/j.sbi.2009.02.003. Epub 2009 Mar 13.
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'.
二十多年来,p53肿瘤抑制蛋白一直是结构生物学面临的一个挑战。完整的p53分子躲过了无数次确定其结构的尝试,大概是由于其内在的构象灵活性,而这种灵活性对该蛋白的功能至关重要。最近通过X射线晶体学、核磁共振光谱和电子显微镜获得的数据,为整个分子的四级结构提供了新的见解,并为研究这些结构如何与“基因组守护者”的细胞和分子生物学相关联提供了新的策略。