1SAE

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAC STRUCTURES)

Replaces:  1SAGReplaces:  1SAI

Summary for 1SAE

• Entry DOI: 10.2210/pdb1sae/pdb
• Descriptor: TUMOR SUPPRESSOR P53 (2 entities in total)
• Functional Keywords: anti-oncogene
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 4
• Total formula weight: 19794.53

Authors

Clore, G.M.,Omichinski, J.G.,Gronenborn, A.M. (deposition date: 1995-03-12, release date: 1995-10-15, Last modification date: 2024-05-22)

Primary citation

Clore, G.M.,Ernst, J.,Clubb, R.,Omichinski, J.G.,Kennedy, W.M.,Sakaguchi, K.,Appella, E.,Gronenborn, A.M.
Refined solution structure of the oligomerization domain of the tumour suppressor p53.
Nat.Struct.Biol., 2:321-333, 1995

PubMed 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.

PubMed: 7796267
DOI: 10.1038/nsb0495-321

Experimental method

SOLUTION NMR