New folds of plant lectins.
Among the crystal structures of lectins determined recently, three--snowdrop lectin, jacalin and amaranthin--represent new lectin families. Their polypeptide folds share remarkably similar features and consist exclusively of beta structure. Autonomously folded beta-sheet subdomains, inter-related by a pseudothreefold symmetry, assemble to form beta-prism or beta-barrel structures which are stabilized by a hydrophobic core.
Wright
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Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond, USA. Christine.Wright@vcu.edu
D019143:Evolution, Molecular; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D037102:Lectins; D010940:Plant Proteins