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| | ==Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist== | | ==Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist== |
| - | <StructureSection load='2nou' size='340' side='right'caption='[[2nou]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2nou' size='340' side='right'caption='[[2nou]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nou]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2NOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scyliorhinus_canicula Scyliorhinus canicula]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NOU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nor|2nor]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2nou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nou OCA], [http://pdbe.org/2nou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nou RCSB], [http://www.ebi.ac.uk/pdbsum/2nou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nou ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nou OCA], [https://pdbe.org/2nou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nou RCSB], [https://www.ebi.ac.uk/pdbsum/2nou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nou ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TKN1_SCYCA TKN1_SCYCA]] Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. | + | [https://www.uniprot.org/uniprot/TKN1_SCYCA TKN1_SCYCA] Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cowsik, S M]] | + | [[Category: Scyliorhinus canicula]] |
| - | [[Category: Dike, A]] | + | [[Category: Cowsik SM]] |
| - | [[Category: 3-10 helix]] | + | [[Category: Dike A]] |
| - | [[Category: Dpc micelle]]
| + | |
| - | [[Category: Helix]]
| + | |
| - | [[Category: Lipid induced conformation]]
| + | |
| - | [[Category: Neuropeptide]]
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| Structural highlights
Function
TKN1_SCYCA Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
Publication Abstract from PubMed
Scyliorhinin I, a linear decapeptide, is the only known tachykinin that shows high affinity for both NK-1 and NK-2 binding sites and low affinity for NK-3 binding sites. As a first step to understand the structure-activity relationship, we report the membrane-induced structure of scyliorhinin I with the aid of circular dichroism and 2D-(1)H NMR spectroscopy. Sequence specific resonance assignments of protons have been made from correlation spectroscopy (TOCSY, DQF-COSY) and NOESY spectroscopy. The interproton distance constraints and dihedral angle constraints have been utilized to generate a family of structures using DYANA. The superimposition of 20 final structures has been reported with backbone pairwise root mean-square deviation of 0.38 +/- 0.19 A. The results show that scyliorhinin I exists in a random coil state in aqueous environments, whereas helical conformation is induced toward the C-terminal region of the peptide (D4-M10) in the presence of dodecyl phosphocholine micelles. Analysis of NMR data is suggestive of the presence of a 3(10)-helix that is in equilibrium with an alpha-helix in this region from residue 4 to 10. An extended highly flexible N-terminus of scyliorhinin I displays some degree of order and a possible turn structure. Observed conformational features have been compared with respect to that of substance P and neurokinin A, which are endogenous agonists of NK-1 and NK-2 receptors, respectively.
Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist.,Dike A, Cowsik SM Biophys J. 2005 May;88(5):3592-600. Epub 2005 Feb 24. PMID:15731392[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dike A, Cowsik SM. Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist. Biophys J. 2005 May;88(5):3592-600. Epub 2005 Feb 24. PMID:15731392 doi:biophysj.104.053231
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