A theoretical study of the structure of parathyroid hormone.
Theoretical analysis of the tertiary and secondary structure of parathyroid hormone was conducted. By combining interpretations from this analysis with chemical data available in the literature, certain structural features of the hormone are consistently predicted. The proposed model for the hormone contains two domains dominated by hydrophobic clustering of critical residues within each domain and separated by an exposed linker region. In the prediction of two domains with a linker region, the model is similar to that proposed by Fiskin et al. [Fiskin, A.M., Cohn, D.M. & Peterson, G.S. (1977) J. Biol. Chem. 252, 8261-8268], but it differs significantly in other respects. The proposed structural features are apparent in the bovine, human, and porcine species of hormone.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006860:Hydrogen Bonding; D008956:Models, Chemical; D010281:Parathyroid Hormone; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship; D013552:Swine
D010281:Parathyroid Hormone