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The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure.
Open accessAbstract
The coordinates of the individual non-hydrogen atoms of the lectin concanavalin A have been determined from the molecular model at 2.0-A resolution and have been adjusted to make them consistent with the known stereochemistry of the constituent amino acid residues. From the coordinates, an analysis has been made of all intra- and intersubunit interactions in the molecule, yielding a description of the hydrogen-bonded structure of the monomer, including two extensive pleated sheet structures and other features of the folding of the polypeptide chain. The description of the noncovalent bonding is extended to include the interactions involved in stabilization of the dimeric and tetrameric structures of the molecule. The complete description of the molecular structure provides a basis for analysis of the biological activities of concanavalin A.
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Cites
Structure of Rhombohedral 2 Zinc Insulin Crystals
ADAMS, M. J., BLUNDELL, T. L., DODSON, E. J., DODSON, G. G., VIJAYAN, M., BAKER, E. N., HARDING, M. M., HODGKIN, D. C., RIMMER, B., & SHEAT, S. (1969) · Nature · doi:10.1038/224491a0 · Cited by 503
Cited by
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,375
Fluorescence-based glucose sensors
Pickup, J. C., Hussain, F., Evans, N. D., Rolinski, O. J., & Birch, D. J. S. (2005) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2004.10.002 · Cited by 616
Glucose sensors: a review of current and emerging technology
Oliver, N. S., Toumazou, C., Cass, A. E. G., & Johnston, D. G. (2009) · Diabetic Medicine · doi:10.1111/j.1464-5491.2008.02642.x · Cited by 584
INFRARED AND LASER‐RAMAN SPECTROSCOPIC STUDIES OF THERMALLY‐INDUCED GLOBULAR PROTEIN GELS
CLARK, A. H., SAUNDERSON, D. H. P., & SUGGETT, A. (1981) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1981.tb02002.x · Cited by 286
Dipoles of the α-helix and β-sheet: their role in protein folding
Hol, W. G. J., Halie, L. M., & Sander, C. (1981) · Nature · doi:10.1038/294532a0 · Cited by 276
Metadata
- Authors
- Reeke, G. N., Becker, J. W., & Edelman, G. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1975-02
- Volume
- 250
- Issue
- 4
- Pages
- 1525-1547
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1525383206
- Cited by
- 362
- References
- 1
- FWCI
- 25.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Reeke, G. N., Becker, J. W., & Edelman, G. M. (1975). The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)41843-7
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