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. 2016 Jun 14:7:228.
doi: 10.3389/fphys.2016.00228. eCollection 2016.

Understanding the Cap Structure in K2P Channels

Affiliations

Understanding the Cap Structure in K2P Channels

Leandro Zúñiga et al. Front Physiol. .
No abstract available

Keywords: K2P channels; K2P potassium channels structure; cap structure; potassium channels; two-pore domain channel.

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Figures

Figure 1
Figure 1
K2P channels: (A) Phylogenetic tree for K2P family (the phylogenic analysis was done with MEGA software version 5). The length of lines indicates the relative distances between nodes and it is scaled below the tree. Numbers on branches indicate bootstrap values (as a percentage). (B) Topological model proposed for K2P channels, each subunit has two pore forming domain (P loops) and four transmembrane domains (denoted M1-M4). (C) Amino acid sequence alignment of K2P channel M1-P1 domain. Gaps are indicated by dashes, letters with black background are identical amino acids, and letters with gray background are similar amino acids. Red arrow indicates the cysteine residues involved in the formation of covalent bridge between two subunits. Amino acid identity (ID) among the M1-P1 domains of hTWIK-1 and the others K2P subunits was calculated. (D) View of the TRAAK structure (PDB code 3UM7) in ribbon representation, showing a non–swapped configuration (conventional configuration). (E) View of the TRAAK structure (PDB code 4I9W) in a domain swapped configuration. The potassium ions are colored orange and the chains are in blue and yellow. The disulfide bridge at the top of the cap is shown in stick representation colored cyan. (F) View from the extracellular side showing the TRAAK pore (PDB code 3UM7). The GYG sequence of each P domain is highlighted in stick representation and the helical cap was removed. For clarity in (D,E), the second pore domain was removed from each TRAAK subunits.

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