1jlo
From Proteopedia
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|PDB= 1jlo |SIZE=350|CAPTION= <scene name='initialview01'>1jlo</scene> | |PDB= 1jlo |SIZE=350|CAPTION= <scene name='initialview01'>1jlo</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlo OCA], [http://www.ebi.ac.uk/pdbsum/1jlo PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1jlo RCSB]</span> | ||
}} | }} | ||
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[[Category: Ireland, C M.]] | [[Category: Ireland, C M.]] | ||
[[Category: Wagoner, R M.Van.]] | [[Category: Wagoner, R M.Van.]] | ||
| - | [[Category: NH2]] | ||
[[Category: amidated c-terminus]] | [[Category: amidated c-terminus]] | ||
[[Category: multiple disulfide bond]] | [[Category: multiple disulfide bond]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:54:14 2008'' |
Revision as of 03:54, 26 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of the Noncompetitive Skeletal Muscle Nicotinic Acetylcholine Receptor Antagonist Psi-conotoxin PIIIE
Overview
A revised, high-resolution structure of psi-conotoxin Piiie (psi-Piiie), a noncompetitive inhibitor of the nicotinic acetylcholine receptor (nAChR), produced through the use of NMR and molecular modeling calculations is presented. The original structures of psi-Piiie had a relatively high degree of disorder, particularly in the conformation of the disulfide bridges. Our studies utilized (13)C-labeling of selected cysteine residues allowing the resolution of all problems of resonance overlap for the cysteine residues. The improved data were used to produce a new set of structures by a molecular modeling process incorporating relaxation matrix methods for the determination of interproton distance restraints and a combination of distance geometry and simulated annealing for structure generation. The structures produced are very well converged with the RMSD of backbone atom positions of the main body of the peptide improving from 0.73 to 0.13 A. Other indicators of correlation with the experimental data and quality of covalent geometry showed significant improvement in the new structures. The overall conformation of the peptide backbone is similar between the two determinations with the exception of the N-terminus. This difference leads to a significant effect on the predicted distribution of positive charge within psi-Piiie, a property likely to influence interpretation of future mutational studies.
About this Structure
1JLO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
An improved solution structure for psi-conotoxin PiiiE., Van Wagoner RM, Ireland CM, Biochemistry. 2003 Jun 3;42(21):6347-52. PMID:12767215
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