ArticleProceedings of the National Academy of Sciences of the United States of America2008
NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Engineering of soluble bacteriorhodopsin.Chemical science · 2025Article
- Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code.Nature communications · 2024Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- QTY code enables design of detergent-free chemokine receptors that retain ligand-binding activities.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Recent advances in automated protein design and its future challenges.Expert opinion on drug discovery · 2018Review
- Solution NMR Studies of Anesthetic Interactions with Ion Channels.Methods in enzymology · 2018Article
- An Exhaustive Search Algorithm to Aid NMR-Based Structure Determination of Rotationally Symmetric Transmembrane Oligomers.Scientific reports · 2017Article
- Membrane proteins: always an insoluble problem?Biochemical Society transactions · 2016Review
- Atomistic insights into human Cys-loop receptors by solution NMR.Biochimica et biophysica acta · 2015Article
- Capturing distinct KCNQ2 channel resting states by metal ion bridges in the voltage-sensor domain.The Journal of general physiology · 2014Article
- Scalable production of highly sensitive nanosensors based on graphene functionalized with a designed G protein-coupled receptor.Nano letters · 2014Article
- Identification of a novel in-frame deletion in KCNQ4 (DFNA2A) and evidence of multiple phenocopies of unknown origin in a family with ADSNHL.European journal of human genetics : EJHG · 2013Article
- A computationally designed water-soluble variant of a G-protein-coupled receptor: the human mu opioid receptor.PloS one · 2013Article
- Binding site and affinity prediction of general anesthetics to protein targets using docking.Anesthesia and analgesia · 2012Article
- NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor.Biochimica et biophysica acta · 2012Article
- Computational design of membrane proteins.Structure (London, England : 1993) · 2012Review
- Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins.Current opinion in chemical biology · 2011Review
- Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY.Biochemistry · 2010Article
- Computational protein design: Advances in the design and redesign of biomolecular nanostructures.Current opinion in colloid & interface science · 2010Article
- Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Chemical reviews · 2010Review
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7 authors.
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Abstract
Structural studies of polytopic membrane proteins are often hampered by the vagaries of these proteins in membrane mimetic environments and by the difficulties in handling them with conventional techniques. Designing and creating water-soluble analogues with preserved native structures offer an attractive alternative. We report here solution NMR studies of WSK3, a water-soluble analogue of the potassium channel KcsA. The WSK3 NMR structure (PDB ID code 2K1E) resembles the KcsA crystal structures, validating the approach. By more stringent comparison criteria, however, the introduction of several charged residues aimed at improving water solubility seems to have led to the possible formations of a few salt bridges and hydrogen bonds not present in the native structure, resulting in slight differences in the structure of WSK3 relative to KcsA. NMR dynamics measurements show that WSK3 is highly flexible in the absence of a lipid environment. Reduced spectral density mapping and model-free analyses reveal dynamic characteristics consistent with an isotropically tumbling tetramer experiencing slow (nanosecond) motions with unusually low local ordering. An altered hydrogen-bond network near the selectivity filter and the pore helix, and the intrinsically dynamic nature of the selectivity filter, support the notion that this region is crucial for slow inactivation. Our results have implications not only for the design of water-soluble analogues of membrane proteins but also for our understanding of the basic determinants of intrinsic protein structure and dynamics.
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