1jlo
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1jlo.gif|left|200px]] | [[Image:1jlo.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1jlo", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1jlo| PDB=1jlo | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Solution Structure of the Noncompetitive Skeletal Muscle Nicotinic Acetylcholine Receptor Antagonist Psi-conotoxin PIIIE''' | '''Solution Structure of the Noncompetitive Skeletal Muscle Nicotinic Acetylcholine Receptor Antagonist Psi-conotoxin PIIIE''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JLO is a [[Single protein]] structure | + | 1JLO is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLO OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 23: | ||
[[Category: Ireland, C M.]] | [[Category: Ireland, C M.]] | ||
[[Category: Wagoner, R M.Van.]] | [[Category: Wagoner, R M.Van.]] | ||
| - | [[Category: | + | [[Category: Amidated c-terminus]] |
| - | [[Category: | + | [[Category: Multiple disulfide bond]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:22:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:22, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 21:22:34 2008
