http://www.sciencedirect.com.ezproxy.hsclib.sunysb.edu/science?_ob=ArticleURL&_udi=B6W81-4GC1R5J-3&_user=334567&_coverDate=10%2F31%2F2005&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000017318&_version=1&_urlVersion=0&_userid=334567&md5=5c696ee8356d440545693b7d60914a00
The function of Kv channels can be described in simple terms using the biophysical properties that determine
1. at which membrane potentials the channels will open,
2. how quickly they open in response to the membrane potential achieving these potentials,
3. if open how long they remain so, and
4. when open at what rate do they allow flux of K+ across the membrane (MacKinnon, 2003). While these inherent biophysical properties are clearly encoded within the primary structure of the particular channel subtype, they can also be modified through post-translational events including covalent modifications (usually phosphorylation) and non-covalent protein–protein interactions (Jonas and Kaczmarek, 1996 and Yi et al., 2001). The biophysical characteristics can also be dramatically modified pharmacologically, a fact that serves as the basis for a diverse array of promising therapeutics (Wickenden, 2002).
http://www.sciencedirect.com.ezproxy.hsclib.sunysb.edu/science?_ob=ArticleURL&_udi=B6T36-49PR9Y1-5&_user=334567&_coverDate=11%2F27%2F2003&_fmt=full&_orig=search&_cdi=4938&view=c&_acct=C000017318&_version=1&_urlVersion=0&_userid=334567&md5=2fd40848628da5e0ffe33c8700ec2db1&ref=full
Therefore, the different kinds of K+ channels open in response to different stimuli: a change in the intracellular Ca2+ concentration, the level of certain G-protein subunits in the cell, or the value of the membrane voltage. Underneath this diversity in gating function, K+ channels have diverse structural domains attached in a modular fashion to the conserved pore unit. Ligand-gated K+ channels typically have cytoplasmic or extracellular domains for binding ligands. Voltage-gated K+ channels have integral membrane domains for sensing voltage differences.
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