1zwa

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[[Image:1zwa.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1zwa", creates the "Structure Box" on the page.
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|GENE= POTENTIAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwa OCA], [http://www.ebi.ac.uk/pdbsum/1zwa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zwa RCSB]</span>
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'''STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''
'''STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''
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[[Category: Marx, U C.]]
[[Category: Marx, U C.]]
[[Category: Roesch, P.]]
[[Category: Roesch, P.]]
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[[Category: disease mutation]]
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[[Category: Disease mutation]]
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[[Category: hormone]]
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[[Category: Hormone]]
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[[Category: signal]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:09:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:42:28 2008''
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Revision as of 15:09, 3 May 2008

Image:1zwa.gif

Template:STRUCTURE 1zwa

STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, 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

1ZWA 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 Sat May 3 18:09:24 2008

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