Recent progress on the structure and function of the TrkH/KtrB ion channel.

Curr Opin Struct Biol

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. Electronic address:

Published: August 2014

AI Article Synopsis

  • Members of the Superfamily of K(+) Transporters (SKT) are crucial for ion uptake in non-animal cells and share similarities with known K(+) channels.
  • Recent crystal structures of SKT proteins, specifically TrkH and KtrB, have uncovered insights into their transport and gating functions.
  • The structures indicate that these proteins have a flexible loop that may serve as a gate, and different conformational changes in associated gating rings suggest varied regulation methods linked to nucleotide binding.

Article Abstract

Members of the Superfamily of K(+) Transporters (SKT) are integral membrane proteins that mediate the uptake of ions into non-animal cells. Although these proteins are homologous to the well-characterized K(+) channel family, relatively little was known about their transport and gating mechanisms until the recent determination of crystal structures for two SKT proteins, TrkH and KtrB. These structures reveal that the SKT proteins are channels, containing a flexible loop in the middle of the permeation pathway that may act as a gate. Two different conformational changes have been observed for the associated gating rings, suggesting different mechanisms of regulation by the binding of nucleotides.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4182332PMC
http://dx.doi.org/10.1016/j.sbi.2014.06.004DOI Listing

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