ArticleBiochimica et biophysica acta2007
Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.iScience · 2023Article
- Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR.Membranes · 2021Review
- pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy.International journal of molecular sciences · 2019Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016Review
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
- FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data.Journal of biomolecular NMR · 2015Article
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.PloS one · 2014Article
- Emerging methodologies to investigate lipid-protein interactions.Integrative biology : quantitative biosciences from nano to macro · 2012Review
- Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Journal of the American Chemical Society · 2011Article
- Solution structure of LC4 transmembrane segment of CCR5.PloS one · 2011Article
- Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration.Journal of molecular biology · 2010Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?Biochemistry · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
KcsA is a homotetrameric 68-kDa membrane-associated potassium channel which selectively gates the flux of potassium ions across the membrane. The channel is known to undergo a pH-dependent open-to-closed transition. Here we describe an NMR study of the monomeric subunit of the channel (KcsAM), solubilized in SDS micelles. Chemical shift, solvent exchange, backbone 15N relaxation and residual dipolar coupling (RDC) data show the TM1 helix to remain intact, but the TM2 helix contains a distinct kink, which is subject to concentration-independent but pH-dependent conformational exchange on a microsecond time scale. The kink region, centered at G99, was previously implicated in the gating of the tetrameric KcsA channel. An RDC-based model of KcsAM at acidic pH orients TM1 and the two helical segments of the kinked TM2 in a configuration reminiscent of the open conformation of the channel. Thus, the transition between states appears to be an inherent capability of the monomer, with the tetrameric assembly exerting a modulatory effect upon the transition which gives the channel its physiological gating profile.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.