2IH3
Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation
Summary for 2IH3
| Entry DOI | 10.2210/pdb2ih3/pdb |
| Related | 2IH1 |
| Descriptor | FAB Heavy Chain, FAB Light Chain, Voltage-gated potassium channel, ... (6 entities in total) |
| Functional Keywords | ion channel d-amino acid semi-synthetic, membrane protein |
| Biological source | Streptomyces lividans More |
| Cellular location | Cell membrane; Multi-pass membrane protein: P0A334 |
| Total number of polymer chains | 3 |
| Total formula weight | 60591.77 |
| Authors | Valiyaveetil, F.I.,Leonetti, M.,Muir, T.W.,MacKinnon, R. (deposition date: 2006-09-25, release date: 2006-11-21, Last modification date: 2024-10-30) |
| Primary citation | Valiyaveetil, F.I.,Leonetti, M.,Muir, T.W.,Mackinnon, R. Ion Selectivity in a Semisynthetic K+ Channel Locked in the Conductive Conformation. Science, 314:1004-1007, 2006 Cited by PubMed Abstract: Potassium channels are K+-selective protein pores in cell membrane. The selectivity filter is the functional unit that allows K+ channels to distinguish potassium (K+) and sodium (Na+) ions. The filter's structure depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+ channel containing the d-enantiomer of alanine in place of a conserved glycine and found by x-ray crystallography that its filter maintains the K+ (conductive) structure in the presence of Na+ and very low concentrations of K+. This channel conducts Na+ in the absence of K+ but not in the presence of K+. These findings demonstrate that the ability of the channel to adapt its structure differently to K+ and Na+ is a fundamental aspect of ion selectivity, as is the ability of multiple K+ ions to compete effectively with Na+ for the conductive filter. PubMed: 17095703DOI: 10.1126/science.1133415 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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