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EMBO J. 2000 Mar 1;19(5):800-6.

The importance of aquaporin water channel protein structures.

Author information

1
M.E.Müller-Institute for Microscopy at the Biozentrum, University of Basel, CH-4056, Switzerland. andreas.engel@unibas.ch

Abstract

The history of the water channel and recent structural and functional analyses of aquaporins are reviewed. These ubiquitous channels are important for bacteria, plants and animals, exhibit a pronounced sequence homology and share functional as well as structural similarities. Aquaporins allow water or small specific solutes to pass unhindered, but block the passage of ions to prevent dissipation of the transmembrane potential. Besides advances in structure determination, recent experiments suggest that many of these channels are regulated by pH variations, phosphorylation and binding of auxiliary proteins.

PMID:
10698922
PMCID:
PMC305620
DOI:
10.1093/emboj/19.5.800
[Indexed for MEDLINE]
Free PMC Article

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