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Cited by 549

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms

Jeffrey, Philip D., Gorina, Svetlana, Pavletich, Nikola P.·1995·Science
DOI 10.1126/science.7878469
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Abstract

The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a β strand and an α helix, associates with a second monomer across an antiparallel β sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer.

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Cites

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Metadata

Authors
Jeffrey, P. D., Gorina, S., & Pavletich, N. P.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1995-03-10
Volume
267
Issue
5203
Pages
1498-1502
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.7878469
OpenAlex
W1996899753
Cited by
549
References
5
FWCI
10.75
Type
journal article
Language
en
Open access
closed

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