4JTD
Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Lys27Met mutant of Charybdotoxin
4JTD の概要
エントリーDOI | 10.2210/pdb4jtd/pdb |
関連するPDBエントリー | 2CRD 2R9R 4JTA 4JTC |
分子名称 | Voltage-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, ... (7 entities in total) |
機能のキーワード | potassium channel, pore blocking toxin, protein-protein complex, trans-enhanced dissociation effect, transport protein-toxin complex, transport protein/toxin |
由来する生物種 | Rattus norvegicus (brown rat,rat,rats) 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 211194.24 |
構造登録者 | Banerjee, A.,Lee, A.,Campbell, E.,MacKinnon, R. (登録日: 2013-03-23, 公開日: 2013-06-12, 最終更新日: 2024-11-20) |
主引用文献 | Banerjee, 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: 23705070DOI: 10.7554/eLife.00594 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.54 Å) |
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