Refined solution structure of the oligomerization domain of the tumour suppressor p53.
The NMR solution structure of the oligomerization domain of the tumour suppressor p53 (residues 319-360) has been refined. The structure comprises a dimer of dimers, oriented in an approximately orthogonal manner. The present structure determination is based on 4,472 experimental NMR restraints which represents a three and half fold increase over our previous work in the number of NOE restraints at the tetramerization interface. A comparison with the recently solved 1.7 A resolution X-ray structure shows that the structures are very similar and that the average angular root-mean-square difference in the interhelical angles is about 1 degree. The results of recent extensive mutagenesis data and the possible effects of mutations which have been identified in human cancers are discussed in the light of the present structure.
Clore
G M
GM
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Ernst
J
J
Clubb
R
R
Omichinski
J G
JG
Kennedy
W M
WM
Sakaguchi
K
K
Appella
E
E
Gronenborn
A M
AM
D000818:Animals; D005075:Biological Evolution; D002247:Carbon Isotopes; D018360:Crystallography, X-Ray; D006801:Humans; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics; D014714:Vertebrates
D002247:Carbon Isotopes; D046911:Macromolecular Substances; D009587:Nitrogen Isotopes; D016159:Tumor Suppressor Protein p53