| Literature DB >> 7796267 |
G M Clore1, J Ernst, R Clubb, J G Omichinski, W M Kennedy, K Sakaguchi, E Appella, A M Gronenborn.
Abstract
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.Entities:
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Year: 1995 PMID： 7796267 DOI： 10.1038/nsb0495-321
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368