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1c4e
From Proteopedia
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|PDB= 1c4e |SIZE=350|CAPTION= <scene name='initialview01'>1c4e</scene> | |PDB= 1c4e |SIZE=350|CAPTION= <scene name='initialview01'>1c4e</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2gur|2GUR]] | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1c4e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c4e RCSB]</span> | ||
}} | }} | ||
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[[Category: sweet taste transduction]] | [[Category: sweet taste transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:14:17 2008'' |
Revision as of 16:14, 30 March 2008
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| Ligands: | |||||||
| Related: | 2GUR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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