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janelia7_blocks-janelia7_biblio_header | block
Quarterly Reviews of Biophysics. 2006 Nov;39(4):361-96. doi: 10.1017/S0033583506004458
The structure of aquaporins. Gonen Lab
Gonen T, Walz T
Note: Research in this publication was not performed at Janelia.
janelia7_blocks-janelia7_biblio_abstract | block
Abstract
The ubiquitous members of the aquaporin (AQP) family form transmembrane pores that are either exclusive for water (aquaporins) or are also permeable for other small neutral solutes such as glycerol (aquaglyceroporins). The purpose of this review is to provide an overview of our current knowledge of AQP structures and to describe the structural features that define the function of these membrane pores. The review will discuss the mechanisms governing water conduction, proton exclusion and substrate specificity, and how the pore permeability is regulated in different members of the AQP family.
PMID: 17156589 [PubMed - indexed for MEDLINE]
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Janelia Authors
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