1ZWC

STRUCTURE OF BOVINE PARATHYROID HORMONE FRAGMENT 1-37, NMR, 10 STRUCTURES

Summary for 1ZWC

• Entry DOI: 10.2210/pdb1zwc/pdb
• Descriptor: PARATHYROID HORMONE (1 entity in total)
• Functional Keywords: hormone, disease mutation
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P01268
• Total number of polymer chains: 1
• Total formula weight: 4400.13

Authors

Roesch, P.,Marx, U.C. (deposition date: 1996-06-17, release date: 1997-03-12, 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

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: 10623601
DOI: 10.1006/bbrc.1999.1958

Experimental method

SOLUTION NMR