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2ca7

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ca7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ca7 OCA], [http://www.ebi.ac.uk/pdbsum/2ca7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ca7 RCSB]</span>
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[[Category: toxin]]
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Revision as of 23:18, 30 March 2008

Image:2ca7.gif


PDB ID 2ca7

Drag the structure with the mouse to rotate
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CONKUNITZIN-S1 IS THE FIRST MEMBER OF A NEW KUNITZ-TYPE NEUROTOXIN FAMILY- STRUCTURAL AND FUNCTIONAL CHARACTERIZATION


Overview

Conkunitzin-S1 (Conk-S1) is a 60-residue neurotoxin from the venom of the cone snail Conus striatus that interacts with voltage-gated potassium channels. Conk-S1 shares sequence homology with Kunitz-type proteins but contains only two out of the three highly conserved cysteine bridges, which are typically found in these small, basic protein modules. In this study the three-dimensional structure of Conk-S1 has been solved by multidimensional NMR spectroscopy. The solution structure of recombinant Conk-S1 shows that a Kunitz fold is present, even though one of the highly conserved disulfide cross-links is missing. Introduction of a third, homologous disulfide bond into Conk-S1 results in a functional toxin with similar affinity for Shaker potassium channels. The affinity of Conk-S1 can be enhanced by a pore mutation within the Shaker channel pore indicating an interaction of Conk-S1 with the vestibule of potassium channels.

About this Structure

2CA7 is a Single protein structure of sequence from Conus striatus. Full crystallographic information is available from OCA.

Reference

Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization., Bayrhuber M, Vijayan V, Ferber M, Graf R, Korukottu J, Imperial J, Garrett JE, Olivera BM, Terlau H, Zweckstetter M, Becker S, J Biol Chem. 2005 Jun 24;280(25):23766-70. Epub 2005 Apr 15. PMID:15833744

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