ArticleProceedings of the National Academy of Sciences of the United States of America2003
A model of the glycine receptor deduced from Brownian dynamics studies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- Engineering aspects of biological ion channels--from biosensors to computational models for permeation.Protoplasma · 2012Review
- Anion currents in yeast K+ transporters (TRK) characterize a structural homologue of ligand-gated ion channels.Pflugers Archiv : European journal of physiology · 2011Article
- Loop 2 structure in glycine and GABA(A) receptors plays a key role in determining ethanol sensitivity.The Journal of biological chemistry · 2009Article
- Molecular basis for cation selectivity in claudin-2-based paracellular pores: identification of an electrostatic interaction site.The Journal of general physiology · 2009Article
- Anion-cation permeability correlates with hydrated counterion size in glycine receptor channels.Biophysical journal · 2008Article
- Roles for loop 2 residues of alpha1 glycine receptors in agonist activation.The Journal of biological chemistry · 2008Article
- Computational prediction of ion permeation characteristics in the glycine receptor modified by photo-sensitive compounds.Journal of computer-aided molecular design · 2008Article
- Probing ion-channel pores one proton at a time.Nature · 2005Article
- Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.Biophysical journal · 2005Article
- Homology model of the GABAA receptor examined using Brownian dynamics.Biophysical journal · 2005Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
We have developed a three-dimensional model of the alpha1 homomeric glycine receptor by using Brownian dynamics simulations to account for its observed physiological properties. The model channel contains a large external vestibule and a shallow internal vestibule, connected by a narrow, cylindrical selectivity filter. Three rings of charged residues from the pore-lining M2 domain are modeled as point charges in the protein. Our simulations reproduce many of the key features of the channel, such as the current-voltage profiles, permeability ratios, and ion selectivity. When we replace the ring of alanine residues lining the selectivity filter with glutamates, the mutant model channel becomes permeable to cations, as observed experimentally. In this mutation, anions act as chaperones for sodium ions in the extracellular vestibule, and together they penetrate deep inside the channel against a steep energy barrier encountered by unaccompanied ions. Two subsequent amino acid mutations increase the cation permeability, enabling monovalent cations to permeate through the channel unaided and divalent cations to permeate when chaperoned by anions. These results illustrate the key structural features and underlying mechanism for charge selectivity in the glycine receptor.
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