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Revision as of 11:17, 8 November 2017
Crystal Structure of the Human BK Gating ApparatusCrystal Structure of the Human BK Gating Apparatus
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHigh-conductance voltage- and Ca2+-activated K+ (BK) channels encode negative feedback regulation of membrane voltage and Ca2+ signaling, playing a central role in numerous physiological processes. We determined the x-ray structure of the human BK Ca2+ gating apparatus at a resolution of 3.0 angstroms and deduced its tetrameric assembly by solving a 6 angstrom resolution structure of a Na+-activated homolog. Two tandem C-terminal regulator of K+ conductance (RCK) domains from each of four channel subunits form a 350-kilodalton gating ring at the intracellular membrane surface. A sequence of aspartic amino acids that is known as the Ca2+ bowl, and is located within the second of the tandem RCK domains, creates four Ca2+ binding sites on the outer perimeter of the gating ring at the "assembly interface" between RCK domains. Functionally important mutations cluster near the Ca2+ bowl, near the "flexible interface" between RCK domains, and on the surface of the gating ring that faces the voltage sensors. The structure suggests that the Ca2+ gating ring, in addition to regulating the pore directly, may also modulate the voltage sensor. Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution.,Yuan P, Leonetti MD, Pico AR, Hsiung Y, MacKinnon R Science. 2010 Jul 9;329(5988):182-6. Epub 2010 May 27. PMID:20508092[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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