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==Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist==
<StructureSection load='2nou' size='340' side='right'caption='[[2nou]]' scene=''>
== Structural highlights ==
<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='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'>[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>
== Function ==
[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.
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== 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<ref>PMID:15731392</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Scyliorhinus canicula]]
[[Category: Cowsik SM]]
[[Category: Dike A]]