5WIE

Crystal structure of a Kv1.2-2.1 chimera K+ channel V406W mutant in an inactivated state

5WIE の概要

• エントリーDOI: 10.2210/pdb5wie/pdb
• 分子名称: Voltage-gated potassium channel subunit beta-2, Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily A member 2, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: ion channel, membrane protein, inactivation, voltage-gated, metal transport
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 201910.43

構造登録者

Pau, V.,Zhou, Y.,Ramu, Y.,Xu, Y.,Lu, Z. (登録日: 2017-07-19, 公開日: 2017-08-30, 最終更新日: 2023-10-04)

主引用文献

Pau, V.,Zhou, Y.,Ramu, Y.,Xu, Y.,Lu, Z.
Crystal structure of an inactivated mutant mammalian voltage-gated K(+) channel.
Nat. Struct. Mol. Biol., 24:857-865, 2017

PubMed Abstract: C-type inactivation underlies important roles played by voltage-gated K (Kv) channels. Functional studies have provided strong evidence that a common underlying cause of this type of inactivation is an alteration near the extracellular end of the channel's ion-selectivity filter. Unlike N-type inactivation, which is known to reflect occlusion of the channel's intracellular end, the structural mechanism of C-type inactivation remains controversial and may have many detailed variations. Here we report that in voltage-gated Shaker K channels lacking N-type inactivation, a mutation enhancing inactivation disrupts the outermost K site in the selectivity filter. Furthermore, in a crystal structure of the Kv1.2-2.1 chimeric channel bearing the same mutation, the outermost K site, which is formed by eight carbonyl-oxygen atoms, appears to be slightly too small to readily accommodate a K ion and in fact exhibits little ion density; this structural finding is consistent with the functional hallmark of C-type inactivation.

PubMed: 28846092
DOI: 10.1038/nsmb.3457

実験手法

X-RAY DIFFRACTION (3.3 Å)