1c4e
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1c4e.png|left|200px]] | ||
- | < | + | ==GURMARIN FROM GYMNEMA SYLVESTRE== |
- | + | <StructureSection load='1c4e' size='340' side='right'caption='[[1c4e]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1c4e]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1C4E FirstGlance]. <br> | |
- | or | + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1c4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4e OCA], [https://pdbe.org/1c4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4e RCSB], [https://www.ebi.ac.uk/pdbsum/1c4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4e ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/GUR_GYMSY GUR_GYMSY] Suppresses strongly the sweet taste responses in the rat with high specificity to sucrose, glucose, glycine, and saccharin. This effect is reversible, but complete recovery of the suppressed responses required at least 3h. Gurmarin showed no effect or only a very weak effect on the sweet taste sensation in humans. | ||
+ | <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> | |
- | + | <div class="pdbe-citations 1c4e" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Gymnema sylvestre]] | [[Category: Gymnema sylvestre]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Dingley AJ]] |
- | [[Category: | + | [[Category: Fletcher JI]] |
- | [[Category: | + | [[Category: King GF]] |
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Current revision
GURMARIN FROM GYMNEMA SYLVESTRE
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