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Lectin Structure
Abstract
Lectins comprise a structurally very diverse class of proteins characterized by their ability to bind carbohydrates with considerable specificity. They are found in organisms ranging from viruses and plants to humans and serve to mediate biological recognition events. Although lectins bind monosaccharides rather weakly, they employ common strategies for enhancing both the affinity and specificity of their interactions for more complex carbohydrate ligands. The terms subsite and subunit multivalency are defined to describe the ways in which these enhancements are achieved. Analysis of the X-ray crystal structures of different lectin types serves to illustrate how, in structural terms, subsite and subunit multivalency confer context-specific functional properties.
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Citations
Cited by
Lectins: Carbohydrate-Specific Proteins That Mediate Cellular Recognition
Lis, H., & Sharon, N. (1998) · Chemical Reviews · doi:10.1021/cr940413g · Cited by 1,760
Sára, M., & Sleytr, U. B. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.4.859-868.2000 · Cited by 766
The repertoire of glycan determinants in the human glycome
Cummings, R. D. (2009) · Molecular BioSystems · doi:10.1039/b907931a · Cited by 487
From lectin structure to functional glycomics: principles of the sugar code
Gabius, H.-J., André, S., Jiménez-Barbero, J., Romero, A., & Solís, D. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.005 · Cited by 483
THE MOLECULAR STRUCTURE OF CELL ADHESION MOLECULES
Chothia, C., & Jones, E. Y. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.823 · Cited by 371
Metadata
- Authors
- Rini, J. M.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 1995-06
- Volume
- 24
- Issue
- 1
- Pages
- 551-577
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W4239828048
- Cited by
- 375
- References
- 0
- FWCI
- 6.99
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rini, J. M. (1995). Lectin Structure. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.bb.24.060195.003003
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