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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Revision as of 02:22, 21 November 2007
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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 NH2 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
Page seeded by OCA on Wed Nov 21 04:29:38 2007
Categories: Single protein | Bernard, C. | Chagot, B. | Corzo, G. | Darbon, H. | Escoubas, P. | Ferrat, G. | Lazdunski, M. | Villegas, E. | NH2 | Toxin