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3IGA

Potassium Channel KcsA-Fab complex in Li+ and K+

Summary for 3IGA
Entry DOI10.2210/pdb3iga/pdb
Related3GB7
DescriptorAntibody Fab Fragment heavy chain, Antibody Fab fragment light chain, Voltage-gated potassium channel, ... (6 entities in total)
Functional Keywordskcsa, lithium, lithium block, potassium channel, membrane protein, cell membrane, ion transport, ionic channel, membrane, transmembrane, transport, voltage-gated channel, transport protein
Biological sourceStreptomyces lividans
More
Cellular locationCell membrane; Multi-pass membrane protein: P0A334
Total number of polymer chains3
Total formula weight60742.27
Authors
Thompson, A.N.,Ilsoo, K.,Panosian, T.D.,Iverson, T.M.,Allen, T.W.,Nimigean, C.M. (deposition date: 2009-07-27, release date: 2009-11-17, Last modification date: 2024-10-09)
Primary citationThompson, A.N.,Kim, I.,Panosian, T.D.,Iverson, T.M.,Allen, T.W.,Nimigean, C.M.
Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore.
Nat.Struct.Mol.Biol., 16:1317-1324, 2009
Cited by
PubMed Abstract: Potassium channels allow K(+) ions to diffuse through their pores while preventing smaller Na(+) ions from permeating. Discrimination between these similar, abundant ions enables these proteins to control electrical and chemical activity in all organisms. Selection occurs at the narrow selectivity filter containing structurally identified K(+) binding sites. Selectivity is thought to arise because smaller ions such as Na(+) do not bind to these K(+) sites in a thermodynamically favorable way. Using the model K(+) channel KcsA, we examined how intracellular Na(+) and Li(+) interact with the pore and the permeant ions using electrophysiology, molecular dynamics simulations and X-ray crystallography. Our results suggest that these small cations have a separate binding site within the K(+) selectivity filter. We propose that selective permeation from the intracellular side primarily results from a large energy barrier blocking filter entry for Na(+) and Li(+) in the presence of K(+), not from a difference of binding affinity between ions.
PubMed: 19946269
DOI: 10.1038/nsmb.1703
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

239149

數據於2025-07-23公開中

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