1BWX
THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES
Summary for 1BWX
| Entry DOI | 10.2210/pdb1bwx/pdb |
| Descriptor | PARATHYROID HORMONE (1 entity in total) |
| Functional Keywords | peptide hormone, solution structure, human parathyroid hormone |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 4537.27 |
| Authors | Marx, U.C.,Roesch, P.,Adermann, K.,Bayer, P.,Forssmann, W.-G. (deposition date: 1998-09-29, release date: 2000-01-14, Last modification date: 2024-05-22) |
| Primary citation | Marx, U.C.,Adermann, K.,Bayer, P.,Forssmann, W.G.,Rosch, P. Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37). Biochem.Biophys.Res.Commun., 267:213-220, 2000 Cited by PubMed Abstract: Parathyroid hormone (PTH) is involved in regulation of the calcium level in blood and has an influence on bone metabolism, thus playing a role in osteoporosis therapy. In this study, the structures of the human PTH fragments (1-34) and (1-39) as well as bovine PTH(1-37) in aqueous buffer solution under near physiological conditions were determined using two-dimensional nuclear magnetic resonance spectroscopy. The overall structure of the first 34 amino acids of these three peptides is virtually identical, exhibiting a short NH(2)-terminal and a longer COOH-terminal helix as well as a defined loop region from His14 to Ser17, stabilized by hydrophobic interactions. bPTH(1-37), which has a higher biological activity, shows a better-defined NH(2)-terminal part. In contrast to NH(2)-terminal truncations, which cause destabilization of helical structure, neither COOH-terminal truncation nor elongation significantly influences the secondary structure. Furthermore, we investigated the structure of hPTH(1-34) in 20% trifluoroethanol solution. In addition to its helix-stabilizing effect, trifluorethanol causes the loss of tertiary hydrophobic interactions. PubMed: 10623601DOI: 10.1006/bbrc.1999.1958 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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