1pet
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NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53
OverviewOverview
We report the solution structure of the minimum transforming domain, (residues 303-366) of human p53 (p53tet) determined by multidimensional, NMR spectroscopy. This domain contains a number of important functions, associated with p53 activity including transformation, oligomerization, nuclear localization and a phosphorylation site for p34/cdc2 kinase., p53tet forms a symmetric dimer of dimers that is significantly different, from a recent structure reported for a shorter construct of this domain., Phosphorylation of Ser 315 has only minor structural consequences, as this, region of the protein is unstructured. Modelling based on the p53tet, structure suggests possible modes of interaction between adjacent domains, in full-length p53 as well as modes of interaction with DNA.
DiseaseDisease
Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]
About this StructureAbout this Structure
1PET is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the tetrameric minimum transforming domain of p53., Lee W, Harvey TS, Yin Y, Yau P, Litchfield D, Arrowsmith CH, Nat Struct Biol. 1994 Dec;1(12):877-90. PMID:7773777
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