1hpy
From Proteopedia
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'''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES''' | '''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES''' | ||
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[[Category: Marx, U C.]] | [[Category: Marx, U C.]] | ||
[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
- | [[Category: | + | [[Category: Human parathyroid hormone]] |
- | [[Category: | + | [[Category: Peptide hormone]] |
- | [[Category: | + | [[Category: Solution structure]] |
- | [[Category: | + | [[Category: Trifluorethanol]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:06:18 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 16:06, 2 May 2008
THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES
Overview
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.
About this Structure
1HPY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37)., Marx UC, Adermann K, Bayer P, Forssmann WG, Rosch P, Biochem Biophys Res Commun. 2000 Jan 7;267(1):213-20. PMID:10623601 Page seeded by OCA on Fri May 2 19:06:18 2008