RGD Reference Report - Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel. - Rat Genome Database

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Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel.

Authors: Banerjee, A  Lee, A  Campbell, E  Mackinnon, R 
Citation: Banerjee A, etal., Elife. 2013 May 21;2:e00594. doi: 10.7554/eLife.00594.
RGD ID: 10047260
Pubmed: PMID:23705070   (View Abstract at PubMed)
PMCID: PMC3660741   (View Article at PubMed Central)
DOI: DOI:10.7554/eLife.00594   (Journal Full-text)

Pore-blocking toxins inhibit voltage-dependent K(+) channels (Kv channels) by plugging the ion-conduction pathway. We have solved the crystal structure of paddle chimera, a Kv channel in complex with charybdotoxin (CTX), a pore-blocking toxin. The toxin binds to the extracellular pore entryway without producing discernable alteration of the selectivity filter structure and is oriented to project its Lys27 into the pore. The most extracellular K(+) binding site (S1) is devoid of K(+) electron-density when wild-type CTX is bound, but K(+) density is present to some extent in a Lys27Met mutant. In crystals with Cs(+) replacing K(+), S1 electron-density is present even in the presence of Lys27, a finding compatible with the differential effects of Cs(+) vs K(+) on CTX affinity for the channel. Together, these results show that CTX binds to a K(+) channel in a lock and key manner and interacts directly with conducting ions inside the selectivity filter. DOI:http://dx.doi.org/10.7554/eLife.00594.001.

Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
voltage-gated potassium channel complex part_ofIDA 10047260PMID:23705070UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Kcna2  (potassium voltage-gated channel subfamily A member 2)


Additional Information