2w0f

Potassium Channel KcsA-Fab Complex with Tetraoctylammonium

spinqualitylabelsall models 2w0f, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w0f is a 3 chain structure with sequence from "actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965 and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CO, DGA, F09, HX0, K Related: 1r3k, 2a9h, 1k4d, 1k4c, 2hg5, 2bob, 1f6g, 2boc, 1jq2, 1r3j, 1jvm, 1jq1, 2ih3, 1zwi, 1bl8, 1r3i, 2ih1, 1j95, 2h8p, 1r3l, 2atk, 4uuj Resources: FirstGlance, OCA, RCSB, PDBsum Function [KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+). 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 PubMed Potassium channels allow for the passive movement of potassium ions across the cell membrane and are instrumental in controlling the membrane potential in all cell types. Quaternary ammonium (QA) compounds block potassium channels and have long been used to study the functional and structural properties of these channels. Here we describe the interaction between three symmetrical hydrophobic QAs and the prokaryotic potassium channel KcsA. The structures demonstrate the presence of a hydrophobic pocket between the inner helices of KcsA and provide insight into the binding site and blocking mechanism of hydrophobic QAs. The structures also reveal a structurally hidden pathway between the central cavity and the outside membrane environment reminiscent of the lateral fenestration observed in sodium channels that can be accessed through small conformational changes in the pore wall. We propose that the hydrophobic binding pocket stabilizes the alkyl chains of long-chain QA molecules and may play a key role in hydrophobic drug binding in general. Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site.,Lenaeus MJ, Burdette D, Wagner T, Focia PJ, Gross A Biochemistry. 2014 Aug 19;53(32):5365-73. doi: 10.1021/bi500525s. Epub 2014 Aug, 8. PMID:25093676 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody Monoclonal Antibody Potassium Channel

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