1n8m: Difference between revisions
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'''Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels''' | {{Structure | ||
|PDB= 1n8m |SIZE=350|CAPTION= <scene name='initialview01'>1n8m</scene> | |||
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|LIGAND= | |||
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'''Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1N8M is a [ | 1N8M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8M OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels., Guijarro JI, M'Barek S, Gomez-Lagunas F, Garnier D, Rochat H, Sabatier JM, Possani L, Delepierre M, Protein Sci. 2003 Sep;12(9):1844-54. PMID:[http:// | Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels., Guijarro JI, M'Barek S, Gomez-Lagunas F, Garnier D, Rochat H, Sabatier JM, Possani L, Delepierre M, Protein Sci. 2003 Sep;12(9):1844-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12930984 12930984] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barek, S M.]] | [[Category: Barek, S M.]] | ||
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[[Category: potassium channel blocker]] | [[Category: potassium channel blocker]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:35 2008'' | ||
Revision as of 13:53, 20 March 2008
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Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels
OverviewOverview
Pi4 is a short toxin found at very low abundance in the venom of Pandinus imperator scorpions. It is a potent blocker of K(+) channels. Like the other members of the alpha-KTX6 subfamily to which it belongs, it is cross-linked by four disulfide bonds. The synthetic analog (sPi4) and the natural toxin (nPi4) have been obtained by solid-phase synthesis or from scorpion venom, respectively. Analysis of two-dimensional (1)H NMR spectra of nPi4 and sPi4 indicates that both peptides have the same structure. Moreover, electrophysiological recordings of the blocking of Shaker B K(+) channels by sPi4 (K(D) = 8.5 nM) indicate that sPi4 has the same blocking activity of nPi4 (K(D) = 8.0 nM), previously described. The disulfide bonds have been independently determined by NMR and structure calculations, and by Edman-degradation/mass-spectrometry identification of peptides obtained by proteolysis of nPi4. Both approaches indicate that the pairing of the half-cystines is (6)C-(27)C, (12)C-(32)C, (16)C-(34)C, and (22)C-(37)C. The structure of the toxin has been determined by using 705 constraints derived from NMR data on sPi4. The structure, which is well defined, shows the characteristic alpha/beta scaffold of scorpion toxins. It is compared to the structure of the other alpha-KTX6 subfamily members and, in particular, to the structure of maurotoxin, which shows a different pattern of disulfide bridges despite its high degree of sequence identity (76%) with Pi4. The structure of Pi4 and the high amounts of synthetic peptide available, will enable the detailed analysis of the interaction of Pi4 with K(+) channels.
About this StructureAbout this Structure
1N8M is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin specific of potassium channels., Guijarro JI, M'Barek S, Gomez-Lagunas F, Garnier D, Rochat H, Sabatier JM, Possani L, Delepierre M, Protein Sci. 2003 Sep;12(9):1844-54. PMID:12930984
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