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4JTC

Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+

Summary for 4JTC
Entry DOI10.2210/pdb4jtc/pdb
Related2CRD 2R9R 4JTA 4JTD
DescriptorVoltage-gated potassium channel subunit beta-2, Potassium voltage-gated channel subfamily A member 2, Potassium voltage-gated channel subfamily B member 1, Potassium channel toxin alpha-KTx 1.1, ... (6 entities in total)
Functional Keywordspotassium channel, pore blocking toxin, protein-protein complex, transport protein-toxin complex, transport protein/toxin
Biological sourceRattus norvegicus (brown rat,rat,rats)
More
Total number of polymer chains5
Total formula weight211942.68
Authors
Banerjee, A.,Lee, A.,Campbell, E.,MacKinnon, R. (deposition date: 2013-03-23, release date: 2013-06-12, Last modification date: 2019-12-25)
Primary citationBanerjee, A.,Lee, A.,Campbell, E.,Mackinnon, R.
Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel.
Elife, 2:e00594-e00594, 2013
Cited by
PubMed Abstract: 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.
PubMed: 23705070
DOI: 10.7554/eLife.00594
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.56 Å)
Structure validation

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