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| - | [[Image:1jzp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1jzp| PDB=1jzp | SCENE= }} | | {{STRUCTURE_1jzp| PDB=1jzp | SCENE= }} |
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| - | '''Modified Peptide A (D18-A1) of the Rabbit Skeletal Dihydropyridine Receptor'''
| + | ===Modified Peptide A (D18-A1) of the Rabbit Skeletal Dihydropyridine Receptor=== |
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| - | ==Overview==
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| - | An alpha-helical II-III loop segment of the dihydropyridine receptor activates the ryanodine receptor calcium-release channel. We describe a novel manipulation in which this agonist's activity is increased by modifying its surface structure to resemble that of a toxin molecule. In a unique system, native beta-sheet scorpion toxins have been reported to activate skeletal muscle ryanodine receptor calcium channels with high affinity by binding to the same site as the lower-affinity alpha-helical dihydropyridine receptor segment. We increased the alignment of basic residues in the alpha-helical peptide to mimic the spatial orientation of active residues in the scorpion toxin, with a consequent 2-20-fold increase in the activity of the alpha-helical peptide. We hypothesized that, like the native peptide, the modified peptide and the scorpion toxin may bind to a common site. This was supported by (i) similar changes in ryanodine receptor channel gating induced by the native or modified alpha-helical peptide and the beta-sheet toxin, a 10-100-fold reduction in channel closed time, with a < or = 2-fold increase in open dwell time and (ii) a failure of the toxin to further activate channels activated by the peptides. These results suggest that diverse structural scaffolds can present similar conformational surface properties to target common receptor sites.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12429019}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12429019 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12429019}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZP OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZP OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: D-isomer]] | | [[Category: D-isomer]] |
| | [[Category: Dhpr]] | | [[Category: Dhpr]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:07:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:33:55 2008'' |
Revision as of 12:33, 29 July 2008
Template:STRUCTURE 1jzp
Modified Peptide A (D18-A1) of the Rabbit Skeletal Dihydropyridine Receptor
Template:ABSTRACT PUBMED 12429019
About this Structure
Full experimental information is available from OCA.
Reference
The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment., Green D, Pace S, Curtis SM, Sakowska M, Lamb GD, Dulhunty AF, Casarotto MG, Biochem J. 2003 Mar 1;370(Pt 2):517-27. PMID:12429019
Page seeded by OCA on Tue Jul 29 15:33:55 2008
