2mce: Difference between revisions
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==Membrane induced structure of the mammalian tachykinin neuropeptide gamma== | ==Membrane induced structure of the mammalian tachykinin neuropeptide gamma== | ||
<StructureSection load='2mce' size='340' side='right' caption='[[2mce | <StructureSection load='2mce' size='340' side='right'caption='[[2mce]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mce]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2mce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MCE FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=2mce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mce OCA], [https://pdbe.org/2mce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mce RCSB], [https://www.ebi.ac.uk/pdbsum/2mce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mce ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TKN1_RABIT TKN1_RABIT] 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 == | ||
| Line 20: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Oryctolagus cuniculus]] | ||
[[Category: | [[Category: Chandrashekar IR]] | ||
[[Category: | [[Category: Cowsik SM]] | ||
[[Category: | [[Category: Ganjiwale A]] | ||
Latest revision as of 09:03, 15 May 2024
Membrane induced structure of the mammalian tachykinin neuropeptide gammaMembrane induced structure of the mammalian tachykinin neuropeptide gamma
Structural highlights
FunctionTKN1_RABIT 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 PubMedNeuropeptide gamma (NPgamma) is a neurokinin-2 (NK-2) receptor selective agonist, which plays an important role in mediation of asthma and elicits a wide range of biological responses like bronchoconstriction, vasodepression and regulation of endocrine functions. The structure determination of this peptide agonist is important in understanding the molecular basis of peptide ligand recognition by the receptor and for rational drug design. In the present study we report the solution structure of NPgamma characterized by circular dichroism (CD) spectropolarimetry and 2D (1)H NMR spectroscopy in both aqueous and membrane mimetic solvents. Effect of calcium ions on the conformation of NPgamma was also studied using CD spectropolarimetry. Sequence-specific resonance assignments of protons have been made with the aid of correlation spectroscopy experiments and nuclear Overhauser effect spectroscopy experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NPgamma prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region of the peptide (K13-M21) in the presence of perdeuterated dodecylphosphocholine micelles, a membrane model system. A type II' beta turn from H9 to R11 precedes the helical core in the C-terminus of NPgamma. N-terminus of NPgamma also displays some degree of order and a possible turn structure. Conformation adopted by NPgamma in presence of lipid micelles represents a structural motif typical of NK-2 selective agonists and is similar to that observed for Neurokinin A in hydrophobic environment. The observed conformational features have been correlated to the binding ability and biological activity of NPgamma. Membrane-induced structure of the mammalian tachykinin neuropeptide gamma.,Chandrashekar IR, Dike A, Cowsik SM J Struct Biol. 2004 Dec;148(3):315-25. PMID:15522780[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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