ArticleJournal of biomolecular NMR2006
Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel.
Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
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- Unusual CytochromeInternational journal of molecular sciences · 2022Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- Intrinsically disordered regions couple the ligand binding and kinase activation of Trk neurotrophin receptors.iScience · 2022Article
- Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel.Nature communications · 2021Article
- Modulation of Toll-like receptor 1 intracellular domain structure and activity by ZnCommunications biology · 2021Article
- Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR.Membranes · 2021Review
- Revising the mechanism of p75NTR activation: intrinsically monomeric state of death domains invokes the "helper" hypothesis.Scientific reports · 2020Article
- Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation.Frontiers in cell and developmental biology · 2020Article
- Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation.Methods in enzymology · 2019Article
- CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions.PloS one · 2018Article
- NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins.Journal of biomolecular NMR · 2017Article
- Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.Journal of biomolecular NMR · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
A set of TROSY-HNCO (tHNCO)-based 3D experiments is presented for measuring (15)N relaxation parameters in large, membrane-associated proteins, characterized by slow tumbling times and significant spectral overlap. Measurement of backbone (15)N R (1), R (1rho), (15)N-{(1)H} NOE, and (15)N CSA/dipolar cross correlation is demonstrated and applied to study the dynamic behavior of the homotetrameric KcsA potassium channel in SDS micelles under conditions where this channel is in the closed state. The micelle-encapsulated transmembrane domain, KcsA(TM), exhibits a high degree of order, tumbling as an oblate ellipsoid with a global rotational correlation time, tau(c) = 38 +/- 2.5 ns, at 50 degrees C and a diffusion anisotropy, Dparallel/Dperpendicular = 0.79+/-0.05, corresponding to an aspect ratio a/b >/= 1.4. The N- and C-terminal intracellular segments of KcsA exhibit considerable internal dynamics (S (2) values in the 0.2-0.45 range), but are distinctly more ordered than what has been observed for unstructured random coils. Relaxation behavior in these domains confirms the position of the C-terminal helix, and indicates that in SDS micelles, this amphiphilic helix does not associate into a stable homotetrameric helical bundle. The relaxation data indicate the absence of elevated backbone dynamics on the ps-ns time scale for the 5-residue selectivity filter, which selects K(+) ions to enter the channel.
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Registered trials
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