1ZWE

STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 4-37, NMR, 10 STRUCTURES

1ZWE の概要

• エントリーDOI: 10.2210/pdb1zwe/pdb
• 分子名称: PARATHYROID HORMONE (1 entity in total)
• 機能のキーワード: hormone, disease mutation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P01270
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4135.86

構造登録者

Roesch, P.,Marx, U.C. (登録日: 1996-06-17, 公開日: 1997-03-12, 最終更新日: 2024-05-22)

主引用文献

Marx, U.C.,Adermann, K.,Bayer, P.,Meyer, M.,Forssmann, W.G.,Rosch, P.
Structure-activity relation of NH2-terminal human parathyroid hormone fragments.
J.Biol.Chem., 273:4308-4316, 1998

PubMed Abstract: Human parathyroid hormone (hPTH) is involved in the regulation of the calcium level in blood. This hormone function is located in the NH2-terminal 34 amino acids of the 84-amino acid peptide hormone and is transduced via the adenylate cyclase and the phosphatidylinositol signaling pathways. It is well known that truncation of the two NH2-terminal amino acids of the hormone leads to complete loss of in vivo normocalcemic function. To correlate loss of calcium level regulatory activity after stepwise NH2-terminal truncation and solution structure, we studied the conformations of fragments hPTH-(2-37), hPTH-(3-37), and hPTH-(4-37) in comparison to hPTH-(1-37) in aqueous buffer solution under near physiological conditions by circular dichroism spectroscopy, two-dimensional nuclear magnetic resonance spectroscopy, and restrained molecular dynamics calculations. All peptides show helical structures and hydrophobic interactions between Leu-15 and Trp-23 that lead to a defined loop region from His-14 to Ser-17. A COOH-terminal helix from Met-18 to at least Leu-28 was found for all peptides. The helical structure in the NH2-terminal part of the peptides was lost in parallel with the NH2-terminal truncation and can be correlated with the loss of calcium regulatory activity.

PubMed: 9468478
DOI: 10.1074/jbc.273.8.4308

実験手法

SOLUTION NMR