1k8v
From Proteopedia
(New page: 200px<br /><applet load="1k8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k8v" /> '''The NMR-derived Conformation of Neuropeptide...) |
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'''The NMR-derived Conformation of Neuropeptide F from Moniezia expansa'''<br /> | '''The NMR-derived Conformation of Neuropeptide F from Moniezia expansa'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of neuropeptide F (NPF), from the flatworm | + | 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== | ==About this Structure== | ||
| - | 1K8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1K8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: npf]] | [[Category: npf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:22 2008'' |
Revision as of 11:31, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 13:31:22 2008
