Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1944636 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 9 Pages |
Abstract
Some algal viruses contain genes that encode proteins with the hallmarks of K+ channels. One feature of these proteins is that they are less than 100 amino acids in size, which make them truly minimal for a K+ channel protein. That is, they consist of only the pore module present in more complex K+ channels. The combination of miniature size and the functional robustness of the viral K+ channels make them ideal model systems for studying how K+ channels work. Here we summarize recent structure/function correlates from these channels, which provide insight into functional properties such as gating, pharmacology and sorting in cells.
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Authors
Gerhard Thiel, Dirk Baumeister, Indra Schroeder, Stefan M. Kast, James L. Van Etten, Anna Moroni,