1K8V

The NMR-derived Conformation of Neuropeptide F from Moniezia expansa

Summary for 1K8V

• Entry DOI: 10.2210/pdb1k8v/pdb
• NMR Information: BMRB: 5192
• Descriptor: NEUROPEPTIDE F (1 entity in total)
• Functional Keywords: neuropeptide f, moniezia expansa, npf, unknown function
• Cellular location: Secreted: P41967
• Total number of polymer chains: 1
• Total formula weight: 4598.25

Authors

Miskolzie, M.,Kotovych, G. (deposition date: 2001-10-25, release date: 2002-06-12, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

SOLUTION NMR