Title : The external TEA binding site and C-type inactivation in voltage-gated potassium channels.

Pub. Date : 2004 Nov

PMID : 15326027






3 Functional Relationships(s)
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1 In both Kv2.1 and Shaker, modification of cysteines at position 380/449 by 2-(trimethylammonium)ethyl methanethiosulfonate (MTSET) proceeded at identical rates in the absence and presence of TEA. Tetraethylammonium potassium voltage-gated channel subfamily B member 1 Homo sapiens
2 Occupancy by TEA completely prevented MTSET modification of a cysteine in the outer-vestibule turret (Kv2.1 position 356/Shaker position 425), which has been shown to interfere with both TEA binding and the interaction of K+ with an external binding site. Tetraethylammonium potassium voltage-gated channel subfamily B member 1 Homo sapiens
3 Occupancy by TEA completely prevented MTSET modification of a cysteine in the outer-vestibule turret (Kv2.1 position 356/Shaker position 425), which has been shown to interfere with both TEA binding and the interaction of K+ with an external binding site. Tetraethylammonium potassium voltage-gated channel subfamily B member 1 Homo sapiens