1k8v
From Proteopedia
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The NMR-derived Conformation of Neuropeptide F from Moniezia expansa
Overview
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.
About this Structure
1K8V is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
The NMR-derived conformation of neuropeptide F from Moniezia expansa., Miskolzie M, Kotovych G, J Biomol Struct Dyn. 2002 Jun;19(6):991-8. PMID:12023801
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