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

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 languageEnglish (US)
Pages (from-to)599-605
Number of pages7
JournalNature
Volume407
Issue number6804
DOIs
StatePublished - Oct 5 2000

ASJC Scopus subject areas

  • General

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