REFINED SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE TUMOR-SUPPRESSOR P53

被引：198

作者：

CLORE, GM ^{[1
]}

ERNST, J ^{[1
]}

CLUBB, R ^{[1
]}

OMICHINSKI, JG ^{[1
]}

KENNEDY, WMP ^{[1
]}

SAKAGUCHI, K ^{[1
]}

APPELLA, E ^{[1
]}

GRONENBORN, AM ^{[1
]}

机构：

[1] NCI,CELL BIOL LAB,BETHESDA,MD 20892

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 04期

关键词：

D O I：

10.1038/nsb0495-321

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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 degrees. 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.

引用

页码：321 / 333

页数：13

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