Linked Life Data

11743202

Source:http://linkedlifedata.com/resource/pubmed/id/11743202

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pubmed-article:11743202pubmed: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.lld:pubmed
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pubmed-article:11743202pubmed:authorpubmed-author:GrubmüllerHHlld:pubmed
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pubmed-article:11743202pubmed:articleTitleWater permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF.lld:pubmed
pubmed-article:11743202pubmed:affiliationTheoretical Molecular Biophysics Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.lld:pubmed
pubmed-article:11743202pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11743202pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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