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Glycoprotein Structural Genomics: Solving the Glycosylation Problem
Open accessAbstract
Glycoproteins present special problems for structural genomic analysis because they often require glycosylation in order to fold correctly, whereas their chemical and conformational heterogeneity generally inhibits crystallization. We show that the "glycosylation problem" can be solved by expressing glycoproteins transiently in mammalian cells in the presence of the N-glycosylation processing inhibitors, kifunensine or swainsonine. This allows the correct folding of the glycoproteins, but leaves them sensitive to enzymes, such as endoglycosidase H, that reduce the N-glycans to single residues, enhancing crystallization. Since the scalability of transient mammalian expression is now comparable to that of bacterial systems, this approach should relieve one of the major bottlenecks in structural genomic analysis.
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Cited by
Ferrara, C., Grau, S., Jäger, C., Sondermann, P., Brünker, P., Waldhauer, I., Hennig, M., Ruf, A., Rufer, A. C., Stihle, M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108455108 · Cited by 770
Crystal structure of a human GABAA receptor
Miller, P. S., & Aricescu, A. R. (2014) · Nature · doi:10.1038/nature13293 · Cited by 710
Self-citationGuvench, O., Mallajosyula, S. S., Raman, E. P., Hatcher, E., Vanommeslaeghe, K., Foster, T. J., Jamison, F. W., & MacKerell, A. D. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200328p · Cited by 699
Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies
Garces, F., Sok, D., Kong, L., McBride, R., Kim, H. J., Saye-Francisco, K. F., Julien, J.-P., Hua, Y., Cupo, A., Moore, J. P., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.009 · Cited by 178
Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein
Healey, E. G., Bishop, B., Elegheert, J., Bell, C. H., Padilla-Parra, S., & Siebold, C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3016 · Cited by 112
Metadata
- Authors
- Chang, V. T., Crispin, M., Aricescu, A. R., Harvey, D. J., Nettleship, J. E., Fennelly, J. A., Yu, C., Boles, K. S., Evans, E. J., Stuart, D. I., Dwek, R. A., Jones, E. Y., Owens, R. J., & Davis, S. J.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 15
- Issue
- 3
- Pages
- 267-273
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2033032481
- Cited by
- 302
- References
- 0
- FWCI
- 9.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Chang, V. T., Crispin, M., Aricescu, A. R., Harvey, D. J., Nettleship, J. E., Fennelly, J. A., Yu, C., Boles, K. S., Evans, E. J., Stuart, D. I., Dwek, R. A., Jones, E. Y., Owens, R. J., & Davis, S. J. (2007). Glycoprotein Structural Genomics: Solving the Glycosylation Problem. Structure. https://doi.org/10.1016/j.str.2007.01.011
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