The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Local Structural Elements in the Mostly Unstructured Transcriptional Activation Domain of Human p53
Open accessAbstract
DNA transcription is initiated by a small regulatory region of transactivators known as the transactivation domain. In contrast to the rapid progress made on the functional aspect of this promiscuous domain, its structural feature is still poorly characterized. Here, our multidimensional NMR study reveals that an unbound full-length p53 transactivation domain, although similar to the recently discovered group of loosely folded proteins in that it does not have tertiary structure, is nevertheless populated by an amphipathic helix and two nascent turns. The helix is formed by residues Thr(18)-Leu(26) (Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu), whereas the two turns are formed by residues Met(40)-Met(44) and Asp(48)-Trp(53), respectively. It is remarkable that these local secondary structures are selectively formed by functionally critical and positionally conserved hydrophobic residues present in several acidic transactivation domains. This observation suggests that such local structures are general features of acidic transactivation domains and may represent "specificity determinants" (Ptashne, M., and Gann, A. A. F. (1997), Nature 386, 569-577) that are important for transcriptional activity.
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“we were able to identify the presence of a single helix turn, populated to ≈30%, consistent with earlier identification of a nascent helix that becomes fully helical on interaction with MDM2 (17, 18).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [17]
In the citing paper
“The TAD was previously reported to be intrinsically disordered with a tendency for helical structure in TAD1 (residues 18–25) (17), which becomes fully helical on binding to MDM2 (18).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [17]
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Cites
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Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312
Transcriptional Regulation in Mammalian Cells by Sequence-Specific DNA Binding Proteins
Mitchell, P. J., & Tjian, R. (1989) · Science · doi:10.1126/science.2667136 · Cited by 3,114
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551
Kay, L., Keifer, P., & Saarinen, T. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00052a088 · Cited by 2,247
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., & Kay, L. E. (1994) · Biochemistry · doi:10.1021/bi00185a040 · Cited by 2,091
Self-citationHow eukaryotic transcriptional activators work
Ptashne, M. (1988) · Nature · doi:10.1038/335683a0 · Cited by 1,825
Cited by
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
Fuxreiter, M., Simon, I., Friedrich, P., & Tompa, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.017 · Cited by 518
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Obradovic, Z., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382
Critical assessment of protein intrinsic disorder prediction
Necci, M., Piovesan, D., Predictors, C., Hoque, M. T., Walsh, I., Iqbal, S., Vendruscolo, M., Sormanni, P., Wang, C., Raimondi, D., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01117-3 · Cited by 343
Metadata
- Authors
- Lee, H., Mok, K. H., Muhandiram, R., Park, K.-H., Suk, J.-E., Kim, D.-H., Chang, J., Sung, Y. C., Choi, K. Y., & Han, K.-H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 275
- Issue
- 38
- Pages
- 29426-29432
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1988565419
- Cited by
- 329
- References
- 59
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lee, H., Mok, K. H., Muhandiram, R., Park, K.-H., Suk, J.-E., Kim, D.-H., Chang, J., Sung, Y. C., Choi, K. Y., & Han, K.-H. (2000). Local Structural Elements in the Mostly Unstructured Transcriptional Activation Domain of Human p53. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m003107200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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