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1hpy
From Proteopedia
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| - | [[Image:1hpy.gif|left|200px]] | + | [[Image:1hpy.gif|left|200px]] |
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| - | '''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1hpy |SIZE=350|CAPTION= <scene name='initialview01'>1hpy</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HPY is a [ | + | 1HPY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10623601 10623601] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trifluorethanol]] | [[Category: trifluorethanol]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:06 2008'' |
Revision as of 09:40, 20 March 2008
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THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES
Contents |
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.
Disease
Known diseases associated with this structure: Hypoparathyroidism, autosomal dominant OMIM:[168450], Hypoparathyroidism, autosomal recessive OMIM:[168450]
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
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