1gur: Difference between revisions

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|PDB= 1gur |SIZE=350|CAPTION= <scene name='initialview01'>1gur</scene>
|PDB= 1gur |SIZE=350|CAPTION= <scene name='initialview01'>1gur</scene>
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|LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
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|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gur OCA], [http://www.ebi.ac.uk/pdbsum/1gur PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gur RCSB]</span>
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[[Category: sweet-taste]]
[[Category: sweet-taste]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:11 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:45 2008''

Revision as of 20:51, 30 March 2008

File:1gur.gif


PDB ID 1gur

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Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



GURMARIN, A SWEET TASTE-SUPPRESSING POLYPEPTIDE, NMR, 10 STRUCTURES


OverviewOverview

The solution structure of gurmarin was studied by two-dimensional proton NMR spectroscopy at 600 MHz. Gurmarin, a 35-amino acid residue polypeptide recently discovered in an Indian-originated tree Gymnema sylvestre, selectively suppresses the neural responses of rat to sweet taste stimuli. Sequence-specific resonance assignments were obtained for all backbone protons and for most of the side-chain protons. The three-dimensional solution structure was determined by simulated-annealing calculations on the basis of 135 interproton distance constraints derived from NOEs, six distance constraints for three hydrogen bonds and 16 dihedral angle constraints derived from coupling constants. A total of 10 structures folded into a well-defined structure with a triple-stranded antiparallel beta-sheet. The average rmsd values between any two structures were 1.65 +/- 0.39 A for the backbone atoms (N, C alpha, C) and 2.95 +/- 0.27 A for all heavy atoms. The positions of the three disulfide bridges, which could not be determined chemically, were estimated to be Cys3-Cys18, Cys10-Cys23 and Cys17-Cys33 on the basis of the NMR distance constraints. This disulfide bridge pattern in gurmarin turned out to be analogous to that in omega-conotoxin and Momordica charantia trypsin inhibitor-II, and the topology of folding was the same as that in omega-conotoxin.

About this StructureAbout this Structure

1GUR is a Single protein structure of sequence from Gymnema sylvestre. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of gurmarin, a sweet taste-suppressing polypeptide., Arai K, Ishima R, Morikawa S, Miyasaka A, Imoto T, Yoshimura S, Aimoto S, Akasaka K, J Biomol NMR. 1995 Apr;5(3):297-305. PMID:7787425

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