ArticleBiophysical chemistry2013
In silico study of Aquaporin V: Effects and affinity of the central pore-occluding lipid.
Article in Biophysical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- Synergistic roles of aquaporin 5 and intra- and extracellular carbonic anhydrases in promoting COThe Journal of physiology · 2026Article
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Cellular Distribution of Brain Aquaporins and Their Contribution to Cerebrospinal Fluid Homeostasis and Hydrocephalus.Biomolecules · 2022Review
- Aquaporins: New players in breast cancer progression and treatment response.Frontiers in oncology · 2022Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Identification of AtHsp90.6 involved in early embryogenesis and its structure prediction by molecular dynamics simulations.Royal Society open science · 2019Article
- Single-channel permeability and glycerol affinity of human aquaglyceroporin AQP3.Biochimica et biophysica acta. Biomembranes · 2019Article
- Computing osmotic permeabilities of aquaporins AQP4, AQP5, and GlpF from near-equilibrium simulations.Biochimica et biophysica acta. Biomembranes · 2017Article
- Aquaporin-5: from structure to function and dysfunction in cancer.Cellular and molecular life sciences : CMLS · 2016Review
- Molecular dynamics simulation and bioinformatics study on chloroplast stromal ridge complex from rice (Oryza sativa L.).BMC bioinformatics · 2016Article
- Computing membrane-AQP5-phosphatidylserine binding affinities with hybrid steered molecular dynamics approach.Molecular membrane biology · 2015Article
- Aquaporins: important but elusive drug targets.Nature reviews. Drug discovery · 2014Review
- Optimizing water permeability through the hourglass shape of aquaporins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Because of its roles in human physiology, Aquaporin V (AQP5), a major intrinsic protein, has been a subject of many in vitro studies. In particular, a 2008 experiment produced its crystal structure at 2.0Å resolution, which is in a tetrameric conformation consisting of four protomers. Each protomer forms an amphipathic pore that is fit for water permeation. The tetramer has a pore along its quasi-symmetry axis formed by quadruplets of hydrophobic residues (every protomer contributes equally to the quadruplets). A lipid, phosphatidylserine (PS6), is bound to AQP5 in the central pore, totally occluding it. A 2009 experiment showed that AQP5 facilitates not only permeation of water but also permeation of hydrophobic gas molecules across the cell membrane. In this article, we present an in silico study of AQP5 to elucidate the effects of PS6's binding to and dissociating from AQP5's central pore. Computing the lipid's chemical-potential along its dissociation path, we find that PS6 inhibits the function of the central pore with an IC(50) in the micromolar range. Examining the central pore and the interstices between two adjacent protomers, we propose that nonpolar gas molecules (O(2)) permeate through AQP5's hydrophobic central pore when un-occluded.
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Registered trials
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