6v3g | pdb_00006v3g

Cryo-EM structure of Ca2+-free hsSlo1 channel

Loading... Status: waiting for Mol* initialization Structural highlights 6v3g is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 6v22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Slo1 is a Ca(2+)- and voltage-activated K(+) channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by auxiliary proteins that confer tissue-specific gating and pharmacological properties. This study presents cryo-EM structures of Slo1 in complex with the auxiliary protein, beta4. Four beta4, each containing two transmembrane helices, encircle Slo1, contacting it through helical interactions inside the membrane. On the extracellular side, b4 forms a tetrameric crown over the pore. Structures with high and low Ca(2+) concentrations show that identical gating conformations occur in the absence and presence of beta4, implying that beta4 serves to modulate the relative stabilities of 'pre-existing' conformations rather than creating new ones. The effects of beta4 on scorpion toxin inhibition kinetics are explained by the crown, which constrains access but does not prevent binding. Molecular structures of the human Slo1 K(+) channel in complex with beta4.,Tao X, MacKinnon R Elife. 2019 Dec 9;8. pii: 51409. doi: 10.7554/eLife.51409. PMID:31815672 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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