1c4e
From Proteopedia
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| - | + | {{STRUCTURE_1c4e| PDB=1c4e | SCENE= }} | |
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'''GURMARIN FROM GYMNEMA SYLVESTRE''' | '''GURMARIN FROM GYMNEMA SYLVESTRE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C4E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gymnema_sylvestre Gymnema sylvestre]. This structure supersedes the now removed PDB entry | + | 1C4E is a [[Single protein]] structure of 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fletcher, J I.]] | [[Category: Fletcher, J I.]] | ||
[[Category: King, G F.]] | [[Category: King, G F.]] | ||
| - | [[Category: | + | [[Category: Cystine knot]] |
| - | [[Category: | + | [[Category: Gurmarin]] |
| - | [[Category: | + | [[Category: Sweet taste suppression]] |
| - | [[Category: | + | [[Category: Sweet taste transduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:19:01 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:19, 2 May 2008
GURMARIN FROM GYMNEMA SYLVESTRE
Overview
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.
About this Structure
1C4E is a Single protein structure of sequence from Gymnema sylvestre. This structure supersedes the now removed PDB entry 2gur. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 12:19:01 2008
