Medrano-Soto, A, Moreno-Hagelsieb, G, McLaughlin, D, Ye, ZS, Hendargo, KJ and Saier, MH (2018) Bioinformatic characterization of the Anoctamin Superfamily of Ca2+-activated ion channels and lipid scramblases. PLoS One, 13 (3). e0192851 - ?.

[img]
Preview
Text
Bioinformatic characterization of the Anoctamin Superfamily of Ca2+-activated ion channels and lipid scramblases.pdf - Published Version
Available under License Creative Commons Attribution.

Download (4MB) | Preview

Abstract

Our laboratory has developed bioinformatic strategies for identifying distant phylogenetic relationships and characterizing families and superfamilies of transport proteins. Results using these tools suggest that the Anoctamin Superfamily of cation and anion channels, as well as lipid scramblases, includes three functionally characterized families: the Anoctamin (ANO), Transmembrane Channel (TMC) and Ca2+-permeable Stress-gated Cation Channel (CSC) families; as well as four families of functionally uncharacterized proteins, which we refer to as the Anoctamin-like (ANO-L), Transmembrane Channel-like (TMC-L), and CSC-like (CSC-L1 and CSC-L2) families. We have constructed protein clusters and trees showing the relative relationships among the seven families. Topological analyses suggest that the members of these families have essentially the same topologies. Comparative examination of these homologous families provides insight into possible mechanisms of action, indicates the currently recognized organismal distributions of these proteins, and suggests drug design potential for the disease-related channel proteins.

Item Type: Article
Additional Information: Copyright: © 2018 Medrano-Soto et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Uncontrolled Keywords: Bioinformatic, Anoctamin Superfamily, Ca2+-activated, ion channels, lipid scramblases.
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Natural Sciences > School of Chemical and Physical Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 03 Mar 2020 16:24
Last Modified: 03 Mar 2020 16:24
URI: http://eprints.keele.ac.uk/id/eprint/7717

Actions (login required)

View Item View Item