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Dynamics-Driven Allostery in Protein Kinases
Open accessAbstract
Protein kinases have very dynamic structures and their functionality strongly depends on their dynamic state. Active kinases reveal a dynamic pattern with residues clustering into semirigid communities that move in µs-ms timescale. Previously detected hydrophobic spines serve as connectors between communities. Communities do not follow the traditional subdomain structure of the kinase core or its secondary structure elements. Instead they are organized around main functional units. Integration of the communities depends on the assembly of the hydrophobic spine and phosphorylation of the activation loop. Single mutations can significantly disrupt the dynamic infrastructure and thereby interfere with long distance allosteric signaling that propagates throughout the whole molecule. Dynamics is proposed to be the underlying mechanism for allosteric regulation in protein kinases.
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Palla, G., Derényi, I., Farkas, I., & Vicsek, T. (2005) · Nature · doi:10.1038/nature03607 · Cited by 5,373
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
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Reversible and adaptive resistance to BRAF(V600E) inhibition in melanoma
Sun, C., Wang, L., Huang, S., Heynen, G. J. J. E., Prahallad, A., Robert, C., Haanen, J., Blank, C., Wesseling, J., Willems, S. M., et al. (2014) · Nature · doi:10.1038/nature13121 · Cited by 888
Structural Basis for Activation and Inhibition of Class I Phosphoinositide 3-Kinases
Vadas, O., Burke, J. E., Zhang, X., Berndt, A., & Williams, R. L. (2011) · Science Signaling · doi:10.1126/scisignal.2002165 · Cited by 299
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Karoulia, Z., Gavathiotis, E., & Poulikakos, P. I. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.79 · Cited by 404
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Xie, T., Saleh, T., Rossi, P., & Kalodimos, C. G. (2020) · Science · doi:10.1126/science.abc2754 · Cited by 266
Structure and Physiological Regulation of AMPK
Yan, Y., Zhou, X. E., Xu, H. E., & Melcher, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113534 · Cited by 254
TNIK inhibition abrogates colorectal cancer stemness
Masuda, M., Uno, Y., Ohbayashi, N., Ohata, H., Mimata, A., Kukimoto-Niino, M., Moriyama, H., Kashimoto, S., Inoue, T., Goto, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms12586 · Cited by 168
Metadata
- Authors
- Kornev, A. P., & Taylor, S. S.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 40
- Issue
- 11
- Pages
- 628-647
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1771087982
- Cited by
- 284
- References
- 4
- FWCI
- 1.95
- Type
- journal article
- Language
- en
- Open access
- green
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