Structural determinants of water permeation through aquaporin-1

Kazuyoshi Murata, Kaoru Mitsuoka, Teruhisa Hiral, Thomas Walz, Peter Agre, J. Bernard Heymann, Andreas Engel, Yoshinori Fujiyoshi

Research output: Contribution to journalArticlepeer-review

1297 Scopus citations


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 languageEnglish (US)
Pages (from-to)599-605
Number of pages7
Issue number6804
StatePublished - Oct 5 2000

ASJC Scopus subject areas

  • General


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