1k8v: Difference between revisions

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[[Image:1k8v.jpg|left|200px]]<br /><applet load="1k8v" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1k8v.jpg|left|200px]]<br /><applet load="1k8v" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1k8v" />

'''The NMR-derived Conformation of Neuropeptide F from Moniezia expansa'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1K8V OCA].

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==

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[[Category: npf]]

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@@ Line 1: / Line 1: @@
-[[Image:1k8v.jpg|left|200px]]<br /><applet load="1k8v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k8v.jpg|left|200px]]<br /><applet load="1k8v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k8v" />
 '''The NMR-derived Conformation of Neuropeptide F from Moniezia expansa'''<br />
 ==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.
+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==
-K8V 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K8V OCA].
+K8V 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==
@@ Line 19: / Line 19: @@
 [[Category: npf]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:57:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:22 2008''