The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
High-Resolution Structure of the Oligomerization Domain of p53 by Multidimensional NMR
Abstract
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel β sheet. One β strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel β sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.
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Citations
Cites
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
Cited by
Kato, S., Han, S.-Y., Liu, W., Otsuka, K., Shibata, H., Kanamaru, R., & Ishioka, C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1431692100 · Cited by 874
p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
Liu, L., Scolnick, D. M., Trievel, R. C., Zhang, H. B., Marmorstein, R., Halazonetis, T. D., & Berger, S. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1202 · Cited by 776
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641
Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
Jeffrey, P. D., Gorina, S., & Pavletich, N. P. (1995) · Science · doi:10.1126/science.7878469 · Cited by 549
How p53 binds DNA as a tetramer
McLure, K. G., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3342 · Cited by 260
Metadata
- Authors
- Clore, G. M., Omichinski, J. G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E., & Gronenborn, A. M.
- Venue
- Science
- Published
- 1994-07-15
- Volume
- 265
- Issue
- 5170
- Pages
- 386-391
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2103262188
- Cited by
- 307
- References
- 2
- FWCI
- 13.92
- Type
- journal article
- Language
- en
- Open access
- closed
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- Clore, G. M., Omichinski, J. G., Sakaguchi, K., Zambrano, N., Sakamoto, H., Appella, E., & Gronenborn, A. M. (1994). High-Resolution Structure of the Oligomerization Domain of p53 by Multidimensional NMR. Science. https://doi.org/10.1126/science.8023159
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