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1zwc
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(New page: 200px<br /><applet load="1zwc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwc" /> '''STRUCTURE OF BOVINE PARATHYROID HORMONE FRAG...)
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Revision as of 05:34, 21 November 2007
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STRUCTURE OF BOVINE PARATHYROID HORMONE FRAGMENT 1-37, 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
1ZWC is a Single protein structure of sequence from Bos taurus. 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
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