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 3.8 Å 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 Å 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.
Original language | English (US) |
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Pages (from-to) | 599-605 |
Number of pages | 7 |
Journal | Nature |
Volume | 407 |
Issue number | 6804 |
DOIs | |
State | Published - Oct 5 2000 |
ASJC Scopus subject areas
- General