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PDBsum entry 1zwc
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References listed in PDB file
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Key reference
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Title
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Solution structures of human parathyroid hormone fragments hpth(1-34) and hpth(1-39) and bovine parathyroid hormone fragment bpth(1-37).
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Authors
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U.C.Marx,
K.Adermann,
P.Bayer,
W.G.Forssmann,
P.Rösch.
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Ref.
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Biochem Biophys Res Commun, 2000,
267,
213-220.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Strukturen verschiedener parathormonfragmente in loesung
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Author
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U.C.Marx.
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Ref.
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bayreuth : university of ...
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