1k8v
From Proteopedia
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| - | [[ | + | ==The NMR-derived Conformation of Neuropeptide F from Moniezia expansa== |
| + | <StructureSection load='1k8v' size='340' side='right' caption='[[1k8v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1k8v]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K8V FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k8v RCSB], [http://www.ebi.ac.uk/pdbsum/1k8v PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Kotovych, G.]] | [[Category: Kotovych, G.]] | ||
[[Category: Miskolzie, M.]] | [[Category: Miskolzie, M.]] | ||
Revision as of 12:03, 28 September 2014
The NMR-derived Conformation of Neuropeptide F from Moniezia expansa
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