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. 1972 Sep;69(9):2580–2584. doi: 10.1073/pnas.69.9.2580

The Covalent and Three-Dimensional Structure of Concanavalin A

Gerald M Edelman 1, Bruce A Cunningham 1, George N Reeke Jr 1, Joseph W Becker 1, Myron J Waxdal 1, John L Wang 1
PMCID: PMC426993  PMID: 4506778

Abstract

The tentative amino-acid sequence and three-dimensional structure of the lectin concanavalin A have been determined. The amino-acid sequence, which was determined chemically, contains 238 residues. The sequences of three short stretches were assigned on the basis of x-ray crystallographic data. Interpretation of an electron density map at 2-Å resolution indicates that the predominant structural element is extended polypeptide chain arranged in two anti-parallel pleated sheets or β-structures. Residues not included in the β-structures are arranged in regions of random coil. One of the pleated sheets contributes extensively to the interactions among the monomers to form both dimers and tetramers. The positions at which Mn2+, Ca2+, and saccharide are bound to the protein, and the point of cleavage for the formation of the naturally occurring fragments A1 and A2, have been tentatively assigned. Both metal-binding sites are at least 20-Å removed from the position at which saccharides are bound. The saccharide-binding site is a deep pocket of approximately 6Å × 7.5Å × 18Å, the inner portion of which is occupied by hydrophobic residues.

Keywords: x-ray crystallography, sequence, 2-Å resolution, binding sites, lectin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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