1n8m: Difference between revisions

Revision as of 11:19, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n8m.png

Template:STRUCTURE 1n8m

Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channelsSolution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels

Template:ABSTRACT PUBMED 12930984

About this StructureAbout this Structure

1N8M is a Single protein structure. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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 {{STRUCTURE_1n8m|  PDB=1n8m  |  SCENE=  }}
-'''Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels'''
+===Solution structure of Pi4, a four disulfide bridged scorpion toxin active on potassium channels===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12930984}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12930984 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12930984}}
 ==About this Structure==
-N8M is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8M OCA].
+N8M is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8M OCA].
 ==Reference==
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 [[Category: Disulfide bridge stabilized alpha beta motif]]
 [[Category: Potassium channel blocker]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:13:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:19:02 2008''