Referenced in: none

Automatically associated channels: Kv10.2 , Kv11.1

Title: [Three-dimensional structure of human Kv10.2 ion channel studied by single particle electron microscopy and molecular modeling].

Authors:

Journal, date & volume: Bioorg. Khim., 2012 Mar-Apr , 38, 177-84

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/22792721

Abstract
Here we present a three-dimensional structure of human voltage gated Kv10.2 ion channel solved at 2.5 nm resolution. We demonstrated that Kv10.2 channel structure is subdivided into two layers. For interpretation of the structure we used the homology modeling, using the transmembrane regions of MlotiK1 channel (C subunit), and cytoplasmic PAS-PAC and cNBD domains of the N-terminal tail of hERG (A subunit) and the bacterial cyclic nucleotide-activated K+ channel binding domain as the templates. The homologous transmembrane part can be fitted into the upper part of the reconstruction. The cytoplasmic domains form the structure, similar to a "hanging gondola", which is connected to the membrane-embedded domain with linkers. The length of linkers allow contacts between C-terminal cNBD domains and N-terminal PAS domains.