6V8Y
Structure of a Sodium Potassium ion Channel
Summary for 6V8Y
Entry DOI | 10.2210/pdb6v8y/pdb |
Descriptor | Potassium channel protein, (4S)-2-METHYL-2,4-PENTANEDIOL, POTASSIUM ION, ... (5 entities in total) |
Functional Keywords | ion channel, membrane protein |
Biological source | Bacillus cereus |
Total number of polymer chains | 2 |
Total formula weight | 22521.74 |
Authors | Roy, R.,Weiss, K.L.,Coates, L. (deposition date: 2019-12-12, release date: 2021-04-14, Last modification date: 2023-10-11) |
Primary citation | Roy, R.N.,Hendriks, K.,Kopec, W.,Abdolvand, S.,Weiss, K.L.,de Groot, B.L.,Lange, A.,Sun, H.,Coates, L. Structural plasticity of the selectivity filter in a nonselective ion channel. Iucrj, 8:421-430, 2021 Cited by PubMed Abstract: The sodium potassium ion channel (NaK) is a nonselective ion channel that conducts both sodium and potassium across the cellular membrane. A new crystallographic structure of NaK reveals conformational differences in the residues that make up the selectivity filter between the four subunits that form the ion channel and the inner helix of the ion channel. The crystallographic structure also identifies a side-entry, ion-conduction pathway for Na permeation that is unique to NaK. NMR studies and molecular dynamics simulations confirmed the dynamical nature of the top part of the selectivity filter and the inner helix in NaK as also observed in the crystal structure. Taken together, these results indicate that the structural plasticity of the selectivity filter combined with the dynamics of the inner helix of NaK are vital for the efficient conduction of different ions through the non-selective ion channel of NaK. PubMed: 33953928DOI: 10.1107/S205225252100213X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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