From Proteopedia
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| - | [[Image:1jlz.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1jlz| PDB=1jlz | SCENE= }} | | {{STRUCTURE_1jlz| PDB=1jlz | SCENE= }} |
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| - | '''Solution Structure of a K+-Channel Blocker from the Scorpion Toxin of Tityus cambridgei'''
| + | ===Solution Structure of a K+-Channel Blocker from the Scorpion Toxin of Tityus cambridgei=== |
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| - | ==Overview==
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| - | A new K(+)-channel blocking peptide identified from the scorpion venom of Tityus cambridgei (Tc1) is composed of 23 amino acid residues linked with three disulfide bridges. Tc1 is the shortest known toxin from scorpion venom that recognizes the Shaker B K(+) channels and the voltage-dependent K(+) channels in the brain. Synthetic Tc1 was produced using solid-phase synthesis, and its activity was found to be the same as that of native Tc1. The pairings of three disulfide bridges in the synthetic Tc1 were identified by NMR experiments. The NMR solution structures of Tc1 were determined by simulated annealing and energy-minimization calculations using the X-PLOR program. The results showed that Tc1 contains an alpha-helix and a 3(10)-helix at N-terminal Gly(4)-Lys(10) and a double-stranded beta-sheet at Gly(13)-Ile(16) and Arg(19)-Tyr(23), with a type I' beta-turn at Asn(17)-Gly(18). Superposition of each structure with the best structure yielded an average root mean square deviation of 0.26 +/- 0.05 A for the backbone atoms and of 1.40 +/- 0.23 A for heavy atoms in residues 2 to 23. The three-dimensional structure of Tc1 was compared with two structurally and functionally related scorpion toxins, charybdotoxin (ChTx) and noxiustoxin (NTx). We concluded that the C-terminal structure is the most important region for the blocking activity of voltage-gated (Kv-type) channels for scorpion K(+)-channel blockers. We also found that some of the residues in the larger scorpion K(+)-channel blockers (31 to 40 amino acids) are not involved in K(+)-channel blocking activity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11790849}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11790849 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11790849}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1JLZ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLZ OCA]. | + | 1JLZ is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLZ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Nmr structure]] | | [[Category: Nmr structure]] |
| | [[Category: Scorpion venom]] | | [[Category: Scorpion venom]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:23:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:27:10 2008'' |
Revision as of 17:27, 1 July 2008
Template:STRUCTURE 1jlz
Solution Structure of a K+-Channel Blocker from the Scorpion Toxin of Tityus cambridgei
Template:ABSTRACT PUBMED 11790849
About this Structure
1JLZ is a Single protein structure. Full experimental information is available from OCA.
Reference
Solution structure of a K(+)-channel blocker from the scorpion Tityus cambridgei., Wang I, Wu SH, Chang HK, Shieh RC, Yu HM, Chen C, Protein Sci. 2002 Feb;11(2):390-400. PMID:11790849
Page seeded by OCA on Tue Jul 1 20:27:10 2008
