Ontology highlight
ABSTRACT:
SUBMITTER: Banerjee A
PROVIDER: S-EPMC3660741 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
Banerjee Anirban A Banerjee Anirban A Lee Alice A Campbell Ernest E Mackinnon Roderick R
eLife 20130521
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-den ...[more]