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Water Permeation Across Biological Membranes: Mechanism and Dynamics of Aquaporin-1 and GlpF
Open accessAbstract
“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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Cited by
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Dietschy, J. M., & Turley, S. D. (2004) · Journal of Lipid Research · doi:10.1194/jlr.r400004-jlr200 · Cited by 1,095
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Marx, D. (2006) · ChemPhysChem · doi:10.1002/cphc.200600128 · Cited by 920
Qu, X., Brame, J., Li, Q., & Alvarez, P. J. J. (2013) · Accounts of Chemical Research · doi:10.1021/ar300029v · Cited by 799
Metadata
- Authors
- de Groot, B. L., & Grubmüller, H.
- Venue
- Science
- Published
- 2001-12-14
- Volume
- 294
- Issue
- 5550
- Pages
- 2353-2357
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2114489396
- Cited by
- 900
- References
- 0
- FWCI
- 12.92
- Type
- journal article
- Language
- en
- Open access
- green
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- de Groot, B. L., & Grubmüller, H. (2001). Water Permeation Across Biological Membranes: Mechanism and Dynamics of Aquaporin-1 and GlpF. Science. https://doi.org/10.1126/science.1066115
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