Analysis and prediction of protein beta-sheet structures by a combinatorial approach.
Analysis of beta-sheet sandwiches (for example immunoglobulin domains) suggests an algorithm that successfully predicts the tertiary fold of these proteins from their sequence and secondary structure. We propose tertiary structures for beta 2-microglobulin and an HLA-B7 antigen fragment. Topological rules are presented that markedly reduce the number of folds for proteins in which a-helices pack against a parallel beta-sheet.
D005075:Biological Evolution; D003201:Computers; D006680:HLA Antigens; D006801:Humans; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D008962:Models, Theoretical; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D001613:beta 2-Microglobulin
D006680:HLA Antigens; D046911:Macromolecular Substances; D001613:beta 2-Microglobulin