1k8v

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(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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[[Image:1k8v.jpg|left|200px]]<br /><applet load="1k8v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k8v" />
 
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'''The NMR-derived Conformation of Neuropeptide F from Moniezia expansa'''<br />
 
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==Overview==
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==The NMR-derived Conformation of Neuropeptide F from Moniezia expansa==
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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.
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<StructureSection load='1k8v' size='340' side='right'caption='[[1k8v]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moniezia_expansa Moniezia expansa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K8V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8v OCA], [https://pdbe.org/1k8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k8v RCSB], [https://www.ebi.ac.uk/pdbsum/1k8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k8v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NPF_MONEX NPF_MONEX] May have an important physiological role in neuroregulation.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12023801</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12023801 12023801]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1k8v" style="background-color:#fffaf0;"></div>
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[[Category: Kotovych, G.]]
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== References ==
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[[Category: Miskolzie, M.]]
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<references/>
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[[Category: NH2]]
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__TOC__
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[[Category: moniezia expansa]]
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</StructureSection>
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[[Category: neuropeptide f]]
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[[Category: Large Structures]]
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[[Category: npf]]
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[[Category: Moniezia expansa]]
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[[Category: Kotovych G]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:57:34 2007''
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[[Category: Miskolzie M]]

Current revision

The NMR-derived Conformation of Neuropeptide F from Moniezia expansa

PDB ID 1k8v

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