1v7f

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(New page: 200px<br /><applet load="1v7f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v7f" /> '''solution structure of phrixotoxin 1'''<br />...)
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[[Image:1v7f.jpg|left|200px]]<br /><applet load="1v7f" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v7f.jpg|left|200px]]<br /><applet load="1v7f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1v7f" />
caption="1v7f" />
'''solution structure of phrixotoxin 1'''<br />
'''solution structure of phrixotoxin 1'''<br />
==Overview==
==Overview==
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Animal toxins block voltage-dependent potassium channels (Kv) either by, occluding the conduction pore (pore blockers) or by modifying the channel, gating properties (gating modifiers). Gating modifiers of Kv channels bind, to four equivalent extracellular sites near the S3 and S4 segments, close, to the voltage sensor. Phrixotoxins are gating modifiers that bind, preferentially to the closed state of the channel and fold into the, Inhibitory Cystine Knot structural motif. We have solved the solution, structure of Phrixotoxin 1, a gating modifier of Kv4 potassium channels., Analysis of the molecular surface and the electrostatic anisotropy of, Phrixotoxin 1 and of other toxins acting on voltage-dependent potassium, channels allowed us to propose a toxin interacting surface that, encompasses both the surface from which the dipole moment emerges and a, neighboring hydrophobic surface rich in aromatic residues.
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Animal toxins block voltage-dependent potassium channels (Kv) either by occluding the conduction pore (pore blockers) or by modifying the channel gating properties (gating modifiers). Gating modifiers of Kv channels bind to four equivalent extracellular sites near the S3 and S4 segments, close to the voltage sensor. Phrixotoxins are gating modifiers that bind preferentially to the closed state of the channel and fold into the Inhibitory Cystine Knot structural motif. We have solved the solution structure of Phrixotoxin 1, a gating modifier of Kv4 potassium channels. Analysis of the molecular surface and the electrostatic anisotropy of Phrixotoxin 1 and of other toxins acting on voltage-dependent potassium channels allowed us to propose a toxin interacting surface that encompasses both the surface from which the dipole moment emerges and a neighboring hydrophobic surface rich in aromatic residues.
==About this Structure==
==About this Structure==
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1V7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V7F OCA].
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1V7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7F OCA].
==Reference==
==Reference==
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:29:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:16 2008''

Revision as of 13:32, 21 February 2008

Image:1v7f.jpg

1v7f

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solution structure of phrixotoxin 1

Overview

Animal toxins block voltage-dependent potassium channels (Kv) either by occluding the conduction pore (pore blockers) or by modifying the channel gating properties (gating modifiers). Gating modifiers of Kv channels bind to four equivalent extracellular sites near the S3 and S4 segments, close to the voltage sensor. Phrixotoxins are gating modifiers that bind preferentially to the closed state of the channel and fold into the Inhibitory Cystine Knot structural motif. We have solved the solution structure of Phrixotoxin 1, a gating modifier of Kv4 potassium channels. Analysis of the molecular surface and the electrostatic anisotropy of Phrixotoxin 1 and of other toxins acting on voltage-dependent potassium channels allowed us to propose a toxin interacting surface that encompasses both the surface from which the dipole moment emerges and a neighboring hydrophobic surface rich in aromatic residues.

About this Structure

1V7F is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus., Chagot B, Escoubas P, Villegas E, Bernard C, Ferrat G, Corzo G, Lazdunski M, Darbon H, Protein Sci. 2004 May;13(5):1197-208. PMID:15096626

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