1K8V

The NMR-derived Conformation of Neuropeptide F from Moniezia expansa

1K8V の概要

• エントリーDOI: 10.2210/pdb1k8v/pdb
• NMR情報: BMRB: 5192
• 分子名称: NEUROPEPTIDE F (1 entity in total)
• 機能のキーワード: neuropeptide f, moniezia expansa, npf, unknown function
• 細胞内の位置: Secreted: P41967
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4598.25

構造登録者

Miskolzie, M.,Kotovych, G. (登録日: 2001-10-25, 公開日: 2002-06-12, 最終更新日: 2024-11-13)

主引用文献

Miskolzie, M.,Kotovych, G.
The NMR-derived conformation of neuropeptide F from Moniezia expansa.
J.Biomol.Struct.Dyn., 19:991-998, 2002

PubMed Abstract: The solution structure of neuropeptide F (NPF), from the flatworm (platyhelminthes) Moniezia expansa, has been determined by (1)H NMR spectroscopy at 800 MHz in 60%/40% CD(3)OH/H(2)O. NPF is the most abundant neuropeptide in platyhelminthes. The secondary structure of NPF contains an alpha helix from residues Lys(14) to Ile(31), while the N terminus, consisting of residues Pro(-2) to Asn(13), and the C-terminus, consisting of residues Gly(32) to Phe(36), are in a random conformation. The structure was calculated by a simulated annealing protocol, and the conformational data are compared to the porcine neuropeptide Y (NPY), a peptide hormone and neurotransmitter. The exact function of NPF is unknown, but structural similarity with porcine NPY indicates that its mode of action is similar. These structural data can serve as a starting point in the design of new antiparasitic drugs.

PubMed: 12023801

実験手法

SOLUTION NMR