3U6N
Open Structure of the BK channel Gating Ring
Summary for 3U6N
| Entry DOI | 10.2210/pdb3u6n/pdb |
| Descriptor | High-Conductance Ca2+-Activated K+ Channel protein, CALCIUM ION (2 entities in total) |
| Functional Keywords | potassium channel, transport protein |
| Biological source | Danio rerio (Zebrafish) More |
| Total number of polymer chains | 8 |
| Total formula weight | 629833.50 |
| Authors | Yuan, P.,MacKinnon, R. (deposition date: 2011-10-12, release date: 2011-12-07, Last modification date: 2024-02-28) |
| Primary citation | Yuan, P.,Leonetti, M.D.,Hsiung, Y.,Mackinnon, R. Open structure of the Ca(2+) gating ring in the high-conductance Ca(2+)-activated K(+) channel. Nature, 481:94-97, 2011 Cited by PubMed Abstract: High-conductance voltage- and Ca(2+)-activated K(+) channels function in many physiological processes that link cell membrane voltage and intracellular Ca(2+) concentration, including neuronal electrical activity, skeletal and smooth muscle contraction, and hair cell tuning. Like other voltage-dependent K(+) channels, Ca(2+)-activated K(+) channels open when the cell membrane depolarizes, but in contrast to other voltage-dependent K(+) channels, they also open when intracellular Ca(2+) concentrations rise. Channel opening by Ca(2+) is made possible by a structure called the gating ring, which is located in the cytoplasm. Recent structural studies have defined the Ca(2+)-free, closed, conformation of the gating ring, but the Ca(2+)-bound, open, conformation is not yet known. Here we present the Ca(2+)-bound conformation of the gating ring. This structure shows how one layer of the gating ring, in response to the binding of Ca(2+), opens like the petals of a flower. The degree to which it opens explains how Ca(2+) binding can open the transmembrane pore. These findings present a molecular basis for Ca(2+) activation of K(+) channels and suggest new possibilities for targeting the gating ring to treat conditions such as asthma and hypertension. PubMed: 22139424DOI: 10.1038/nature10670 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.61 Å) |
Structure validation
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