Structural highlights
Function
KCAB2_RAT Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Publication Abstract from PubMed
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.
Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel.,Banerjee A, Lee A, Campbell E, Mackinnon R Elife. 2013 May 21;2:e00594. doi: 10.7554/eLife.00594. Print 2013. PMID:23705070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Banerjee A, Lee A, Campbell E, Mackinnon R. Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel. Elife. 2013 May 21;2:e00594. doi: 10.7554/eLife.00594. Print 2013. PMID:23705070 doi:10.7554/eLife.00594
