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Spatial Structure of the Dimeric Transmembrane Domain of the Growth Factor Receptor ErbB2 Presumably Corresponding to the Receptor Active State
Open accessAbstract
Proper lateral dimerization of the transmembrane domains of receptor tyrosine kinases is required for biochemical signal transduction across the plasma membrane. The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer. ErbB2 transmembrane segments associate in a right-handed alpha-helical bundle through the N-terminal tandem GG4-like motif Thr652-X3-Ser656-X3-Gly660, providing an explanation for the pathogenic power of some oncogenic mutations.
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Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
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
Cited by
The ERBB network: at last, cancer therapy meets systems biology
Yarden, Y., & Pines, G. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3309 · Cited by 988
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
Jura, N., Endres, N. F., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J. (2009) · Cell · doi:10.1016/j.cell.2009.04.025 · Cited by 606
A Structural Perspective on the Regulation of the Epidermal Growth Factor Receptor
Kovacs, E., Zorn, J. A., Huang, Y., Barros, T., & Kuriyan, J. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034402 · Cited by 371
The Magic of Bicelles Lights Up Membrane Protein Structure
Dürr, U. H. N., Gildenberg, M., & Ramamoorthy, A. (2012) · Chemical Reviews · doi:10.1021/cr300061w · Cited by 362
Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310
Metadata
- Authors
- Bocharov, E. V., Mineev, K. S., Volynsky, P. E., Ermolyuk, Y. S., Tkach, E. N., Sobol, A. G., Chupin, V. V., Kirpichnikov, M. P., Efremov, R. G., & Arseniev, A. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-03
- Volume
- 283
- Issue
- 11
- Pages
- 6950-6956
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2020202943
- Cited by
- 208
- References
- 3
- FWCI
- 9.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Bocharov, E. V., Mineev, K. S., Volynsky, P. E., Ermolyuk, Y. S., Tkach, E. N., Sobol, A. G., Chupin, V. V., Kirpichnikov, M. P., Efremov, R. G., & Arseniev, A. S. (2008). Spatial Structure of the Dimeric Transmembrane Domain of the Growth Factor Receptor ErbB2 Presumably Corresponding to the Receptor Active State. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m709202200
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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.