Structure and function of water channels

Yoshinori Fujiyoshi, Kaoru Mitsuoka, Bert L. De Groot, Ansgar Philippsen, Helmut Grubmüller, Peter Agre, Andreas Engel

Research output: Contribution to journalReview articlepeer-review

Abstract

Aquaporins comprise a family of water-transforming membrane proteins. All aquaporins are efficient water transporters, while sustaining strict selectivity, even against protons, thereby maintaining the proton gradient across the cell membrane. Recently solved structures of these membrane channels have helped us to understand this remarkable property. The structure of the Escherichia coli glycerol facilitator GlpF at 2.2 Å resolution has enabled the refinement of a low-resolution human aquaporin-1 structure. This latter structure has recently been confirmed by the 2.2 Å structure of bovine aquaporin-1. Further insights, particularly with respect to the dynamics of water permeation and the filter mechanism, have come from recent molecular dynamics simulations.

Original languageEnglish (US)
Pages (from-to)509-515
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume12
Issue number4
DOIs
StatePublished - Aug 1 2002

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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