The Different Families of Ligand-gated Ion Channels

2426 Words5 Pages

Ion channels are macromolecular protein structures which form pores within the membrane of cells to enable the movement of ions into and out of cells, and is the basis of fundamental process such as establishing a resting potential, generation of action potentials etc. In order for the channel to be involved in these cell functions it must possess certain features such as ionic specificity, gating mechanism (i.e. voltage or ligand binding), for these reasons, channels have been the subject of much research over the past few decades.

All ion channels are described as having 2 common functional properties, a selective filter which determines the specificity of the channel and a gate which opens under specific conditions; in addition, these channels can be classified into 2 groups depending of the type of gating mechanism, i.e. voltage or ligand gated. {{Hucho,Ferdinand 2001}}

Ligand-gated ion channels, (which is the focus of this essay) are activated when a certain ligand(s) bind to an extracellular binding site causing the receptor to undergo a conformational change, resulting in the opening of the pore, thus ion flow through, down the electrochemical gradient.

The term ligand gated ion channel (LGIC) is a general term used to describe 3 ‘superfamilies’ of ion channels; Cysteine-loop receptors, Ionotropic Glutamate receptors (IGluR) and ATP-gated ion channels. All these superfamiles can be further split into families of receptors.

Members of a superfamily differ from member of a family. The term family is used to describe receptors that are similar in structure as they are coded for by similar genes, whereas superfamilies are different from each other in structure and function, but evolves from a common ancestor, thus they mu...

... middle of paper ...

...em.2011 Mar;116(5):734-41.Doi: 10.1111/j.1471-4159.2010.07060.x.Epub 2011 Jan 13.
Tu, A.H., Fulgham, R.L., McCrory, M.A., Briles, D.E., Szalai, A.J., 1999. Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae. Infection and Immunity. 67, 4720-4724.
A representation of P2X subunit structure and function. (n.d.). Retrieved December 4, 2013, from Nature: http://www.nature.com/nrn/journal/v2/n3/fig_tab/nrn0301_165a_F2.html
Cys-loop receptor channel structure . (n.d.). Retrieved December 4, 2013, from Nature: http://www.nature.com/nchembio/journal/v8/n12/fig_tab/nchembio.1115_F1.html
Glutamate Receptors . (n.d.). Retrieved December 4, 2013, from University of Bristol: http://www.bris.ac.uk/synaptic/receptors/
Rang, H. P., Dale, M. M., Ritter, J. M., Flower, R. J., & Henderson, G. (2012). Pharmacology (7 ed.). London: Elsevier Inc.

Open Document