4bgc | pdb_00004bgc

T1 domain of the renal potassium channel Kv1.3

spinqualitylabelsall models 4bgc, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bgc is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KCNA3_HUMAN] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Publication Abstract from PubMed Here we present the structure of the T1 domain derived from the voltage-dependent potassium channel Kv1.3 of Homo sapiens sapiens at 1.2 A resolution crystallized under near-physiological conditions. The crystals were grown without precipitant in 150 mM KPi, pH 6.25. The crystals show I4 symmetry typical of the natural occurring tetrameric assembly of the single subunits. The obtained structural model is based on the highest resolution currently achieved for tetramerization domains of voltage-gated potassium channels. We identified an identical fold of the monomer but inside the tetramer the single monomers show a significant rotation which leads to a different orientation of the tetramer compared to other known structures. Such a rotational movement inside the tetrameric assembly might influence the gating properties of the channel. In addition we see two distinct side chain configurations for amino acids located in the top layer proximal to the membrane (Tyr109, Arg116, Ser129, Glu140, Met142, Arg146), and amino acids in the bottom layer of the T1-domain distal from the membrane (Val55, Ile56, Leu77, Arg86). The relative populations of these two states are ranging from 50:50 for Val55, Tyr109, Arg116, Ser129, Glu140, 60:40 for Met142, 65:35 for Arg86, 70:30 for Arg146, and 80:20 for Ile56 and Leu77. The data suggest that in solution these amino acids are involved in an equilibrium of conformational states that may be coupled to the functional states of the whole potassium channel. 1.2 A X-ray Structure of the Renal Potassium Channel K1.3 T1 Domain.,Kremer W, Weyand M, Winklmeier A, Schreier C, Kalbitzer HR Protein J. 2013 Oct 11. PMID:24114469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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