Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HPY

THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34 IN 20% TRIFLUORETHANOL, NMR, 10 STRUCTURES

Summary for 1HPY
Entry DOI10.2210/pdb1hpy/pdb
DescriptorPARATHYROID HORMONE (1 entity in total)
Functional Keywordspeptide hormone, solution structure, human parathyroid hormone, trifluorethanol
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight4125.78
Authors
Marx, U.C.,Roesch, P.,Adermann, K.,Bayer, P.,Forssmann, W.-G. (deposition date: 1998-09-30, release date: 2000-01-14, Last modification date: 2024-05-22)
Primary citationMarx, U.C.,Adermann, K.,Bayer, P.,Forssmann, W.G.,Rosch, P.
Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37).
Biochem.Biophys.Res.Commun., 267:213-220, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10623601
DOI: 10.1006/bbrc.1999.1958
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon