1c4e
From Proteopedia
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| - | [[ | + | ==GURMARIN FROM GYMNEMA SYLVESTRE== |
| + | <StructureSection load='1c4e' size='340' side='right' caption='[[1c4e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1c4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gymnema_sylvestre Gymnema sylvestre]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gur 2gur]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4E FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gur|2gur]]</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=1c4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4e RCSB], [http://www.ebi.ac.uk/pdbsum/1c4e PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gurmarin is a 35-residue polypeptide from the Asclepiad vine Gymnema sylvestre. It has been utilised as a pharmacological tool in the study of sweet-taste transduction because of its ability to selectively inhibit the neural response to sweet tastants in rats. We have chemically synthesised and folded gurmarin and determined its three-dimensional solution structure to high resolution using two-dimensional NMR spectroscopy. Structure calculations utilised 612 interproton-distance, 19 dihedral-angle, and 18 hydrogen-bond restraints. The structure is well defined for residues 3-34, with backbone and heavy atom rms differences of 0.27 +/- 0.09 A and 0.73 +/- 0.09 A, respectively. Gurmarin adopts a compact structure containing an antiparallel beta-hairpin (residues 22-34), several well-defined beta-turns, and a cystine-knot motif commonly observed in toxic and inhibitory polypeptides. Despite striking structural homology with delta-atracotoxin, a spider neurotoxin known to slow the inactivation of voltage-gated Na+ channels, we show that gurmarin has no effect on a variety of voltage-sensitive channels. | ||
| - | + | High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide.,Fletcher JI, Dingley AJ, Smith R, Connor M, Christie MJ, King GF Eur J Biochem. 1999 Sep;264(2):525-33. PMID:10491100<ref>PMID:10491100</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Gymnema sylvestre]] | [[Category: Gymnema sylvestre]] | ||
[[Category: Dingley, A J.]] | [[Category: Dingley, A J.]] | ||
Revision as of 17:12, 20 August 2014
GURMARIN FROM GYMNEMA SYLVESTRE
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