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Structural determinants of water permeation through aquaporin-1

By Y Fujiyoshi, A Engel, JB Heymann, Peter Agre, T Walz, T Hirai, K Mitsuoka and K Murata

Abstract

Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.

Topics: Water/chemistry, Aquaporins/chemistry
Publisher: Nature Publishing Group
Year: 2000
DOI identifier: 10.1038/35036519
OAI identifier: oai:jscholarship.library.jhu.edu:1774.2/34112
Provided by: JScholarship
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