The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies
Open accessAbstract
The three-dimensional structure of the anti-apoptotic protein Bcl-xL complexed to a 25-residue peptide from the death promoting region of Bad was determined using NMR spectroscopy. Although the overall structure is similar to Bcl-xL bound to a 16-residue peptide from the Bak protein (Sattler et al., 1997), the Bad peptide forms additional interactions with Bcl-xL. However, based upon site-directed mutagenesis experiments, these additional contacts do not account for the increased affinity of the Bad 25-mer for Bcl-xL compared to the Bad 16-mer. Rather, the increased helix propensity of the Bad 25-mer is primarily responsible for its greater affinity for Bcl-xL. Based on this observation, a pair of 16-residue peptides were designed and synthesized that were predicted to have a high helix propensity while maintaining the interactions important for complexation with Bcl-xL. Both peptides showed an increase in helix propensity compared to the wild-type and exhibited an enhanced affinity for Bcl-xL.
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Cites
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Muñoz, V., & Serrano, L. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0023 · Cited by 354 · cited 3×
“Individual residues of the Bad 16-mer, which are not involved in protein binding, were sequentially modified with in-house written software, and each mutant peptide was then evaluated for helix propensity using the program AGADIR~Muñoz & Serrano, 1995a, 1995b!.”
BackgroundMethodMuñoz, V., & Serrano, L. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0024 · Cited by 251 · cited 3×
“Individual residues of the Bad 16-mer, which are not involved in protein binding, were sequentially modified with in-house written software, and each mutant peptide was then evaluated for helix propensity using the program AGADIR~Muñoz & Serrano, 1995a, 1995b!.”
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Cited by
Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816
BCL-2 family proteins: changing partners in the dance towards death
Kale, J., Osterlund, E. J., & Andrews, D. W. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137
The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models
Kotschy, A., Szlavik, Z., Murray, J., Davidson, J., Maragno, A. L., Le Toumelin-Braizat, G., Chanrion, M., Kelly, G. L., Gong, J.-N., Moujalled, D. M., et al. (2016) · Nature · doi:10.1038/nature19830 · Cited by 1,047
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
Metadata
- Authors
- PETROS, A. M., NETTESHEIM, D. G., WANG, Y., OLEJNICZAK, E. T., MEADOWS, R. P., MACK, J., SWIFT, K., MATAYOSHI, E. D., ZHANG, H., THOMPSON, C. B., & FESIK, S. W.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2000-12
- Volume
- 9
- Issue
- 12
- Pages
- 2528-2534
- ISSN
- 0961-8368 (ISSN-L)
- OpenAlex
- W2014985938
- Cited by
- 412
- References
- 4
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- green
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- PETROS, A. M., NETTESHEIM, D. G., WANG, Y., OLEJNICZAK, E. T., MEADOWS, R. P., MACK, J., SWIFT, K., MATAYOSHI, E. D., ZHANG, H., THOMPSON, C. B., & FESIK, S. W. (2000). Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Science. https://doi.org/10.1017/s096183680000331x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
