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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5550
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pubmed:dateCreated |
2001-12-14
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pubmed:abstractText |
"Real time" molecular dynamics simulations of water permeation through human aquaporin-1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. We obtained time-resolved, atomic-resolution models of the permeation mechanism across these highly selective membrane channels. Both proteins act as two-stage filters: Conserved fingerprint [asparagine-proline-alanine (NPA)] motifs form a selectivity-determining region; a second (aromatic/arginine) region is proposed to function as a proton filter. Hydrophobic regions near the NPA motifs are rate-limiting water barriers. In AQP1, a fine-tuned water dipole rotation during passage is essential for water selectivity. In GlpF, a glycerol-mediated "induced fit" gating motion is proposed to generate selectivity for glycerol over water.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2353-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11743202-Amino Acid Motifs,
pubmed-meshheading:11743202-Aquaporin 1,
pubmed-meshheading:11743202-Aquaporins,
pubmed-meshheading:11743202-Bacterial Outer Membrane Proteins,
pubmed-meshheading:11743202-Cell Membrane Permeability,
pubmed-meshheading:11743202-Computer Simulation,
pubmed-meshheading:11743202-Crystallography, X-Ray,
pubmed-meshheading:11743202-Escherichia coli Proteins,
pubmed-meshheading:11743202-Glycerol,
pubmed-meshheading:11743202-Hydrogen Bonding,
pubmed-meshheading:11743202-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:11743202-Kinetics,
pubmed-meshheading:11743202-Lipid Bilayers,
pubmed-meshheading:11743202-Membrane Potentials,
pubmed-meshheading:11743202-Models, Biological,
pubmed-meshheading:11743202-Models, Molecular,
pubmed-meshheading:11743202-Permeability,
pubmed-meshheading:11743202-Protein Conformation,
pubmed-meshheading:11743202-Protein Structure, Secondary,
pubmed-meshheading:11743202-Protons,
pubmed-meshheading:11743202-Static Electricity,
pubmed-meshheading:11743202-Thermodynamics,
pubmed-meshheading:11743202-Time Factors,
pubmed-meshheading:11743202-Water
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pubmed:year |
2001
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pubmed:articleTitle |
Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF.
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pubmed:affiliation |
Theoretical Molecular Biophysics Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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