PDBsum entry 1hpy

Peptide hormone

PDB id: 1hpy

Contents

Protein chain

34 a.a. *

* Residue conservation analysis

PDB id:

1hpy

Name:

Peptide hormone

Title:

The solution structure of human parathyroid hormone fragment 1-34 in 20% trifluorethanol, nmr, 10 structures

Structure:

Parathyroid hormone. Chain: a. Fragment: residues 1-34. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

10 models

Authors:

U.C.Marx,P.Roesch,K.Adermann,P.Bayer,W.-G.Forssmann

Key ref:

U.C.Marx et al. (2000). 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. PubMed id: 10623601 DOI: 10.1006/bbrc.1999.1958

Date:

30-Sep-98 Release date: 14-Jan-00

Protein chain

P01270  (PTHY_HUMAN) -  Parathyroid hormone from Homo sapiens

Seq: 115 a.a.

Struc: 34 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1006/bbrc.1999.1958

Biochem Biophys Res Commun 267:213-220 (2000)

PubMed id: 10623601

Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37).

U.C.Marx, K.Adermann, P.Bayer, W.G.Forssmann, P.Rösch.

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.