The current of the outward K+ channel in the cell of horseradish treated with La3+ and the direct interaction between La3+ and the K+ channel protein were investigated using the whole-cell patch-clamp technique, molecular dynamics simulation, and quantum chemistry calculation methods. It was found for the first time that La3+ decreases the current of the K+ channel in the horseradish mesophyll cell. The decrease results from the formation of a coordination bond and hydrogen bond between La3+ and the K+ channel protein in the plasma membrane. The direct interaction destroys the native structure of the K+ channel protein, disturbing the function of the K+ channel protein in the cells. The results can provide the theoretical foundation for understanding the interaction between metal ions (especially high-valence metal ions) and the channel protein in organisms, including animal and plant cells.
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http://dx.doi.org/10.1007/s00775-010-0688-0 | DOI Listing |
Biochemistry
January 2025
BHF Centre of Research Excellence, School of Medicine and Life Sciences, King's College London, London SE1 9NH, United Kingdom.
Transmembrane glucose transport, facilitated by glucose transporters (GLUTs), is commonly understood through the simple mobile carrier model (SMCM), which suggests that the central binding site alternates exposure between the inside and outside of the cell, facilitating glucose exchange. An alternative "multisite model" posits that glucose transport is a stochastic diffusion process between ligand-operated gates within the transporter's central channel. This study aims to test these models by conducting atomistic molecular dynamics simulations of multiple glucose molecules docked along the central cleft of GLUT1 at temperatures both above and below the lipid bilayer melting point.
View Article and Find Full Text PDFBiochem Soc Trans
January 2025
Departamento de Ciencias Médicas Básicas, Facultad de Ciencias de la Salud-sección Medicina, Universidad de La Laguna, Tenerife, ES-38071, Spain.
Large conductance voltage- and calcium-activated potassium channels (BK channels) are extensively found throughout the central nervous system and play a crucial role in various neuronal functions. These channels are activated by a combination of cell membrane depolarisation and an increase in intracellular calcium concentration, provided by calcium sources located close to BK. In 2001, Isaacson and Murphy first demonstrated the coupling of BK channels with N-methyl-D-aspartate receptors (NMDAR) in olfactory bulb neurons.
View Article and Find Full Text PDFExtremophiles
January 2025
Microbiology Laboratory, Department of Botany (DST-FIST and UGC-DRS Funded), Institute of Science, Visva-Bharati (A Central University), Santiniketan, West Bengal, 731235, India.
To fish-out novel salt-tolerance genes, metagenomic DNA of moderately saline sediments of India's largest hypersaline Sambhar Lake was cloned in fosmid. Two functionally-picked clones helped the Escherichia coli host to tolerate 0.6 M NaCl.
View Article and Find Full Text PDFExp Appl Acarol
January 2025
Faculty of Science, Department of Molecular Biology and Genetics, Mugla Sıtkı Koçman University, Mugla, Türkiye.
The Varroa destructor (hereafter referred to as Varroa) is a major pest of honeybees that is generally controlled using pyrethroid-based acaricides. However, resistance to these insecticides has become a growing problem, driven by the acquisition of knockdown resistance (kdr) mutations in the mite's voltage-gated sodium channel (vgsc) gene. Resistance mutations in the vgsc gene, such as the L925V mutation, can confer resistance to pyrethroids like flumethrin and tau-fluvalinate.
View Article and Find Full Text PDFBio Protoc
January 2025
School of Systems Biology, George Mason University, Fairfax, VA, USA.
Nicotinic acetylcholine receptors (nAChRs) are a family of ligand-gated ion channels expressed in nervous and non-nervous system tissue important for memory, movement, and sensory processes. The pharmacological targeting of nAChRs, using small molecules or peptides, is a promising approach for the development of compounds for the treatment of various human diseases including inflammatory and neurogenerative disorders such as Alzheimer's disease. Using the acetylcholine binding protein (Ac-AChBP) as an established structural surrogate for human homopentameric α7 nAChRs, we describe an innovative protein painting mass spectrometry (MS) method that can be used to identify interaction sites for various ligands at the extracellular nAChR site.
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