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Structural insights into aquaporin selectivity and regulation.

Kreida, Stefan LU and Horsefield, Susanna LU (2015) In Current Opinion in Structural Biology 33. p.126-134
Abstract
Aquaporins have emerged as one of the structurally best-characterized membrane protein families, with fourteen different structures available from a diverse range of organisms. While all aquaporins share the same fold and passive mechanism for water permeation, structural details allow for differences in selectivity and modes of regulation. These details are now the emphasis of aquaporin structural biology. Recent structural studies of eukaryotic aquaporins have revealed reoccurring structural themes in both gating and trafficking, implying a limited number of structural solutions to aquaporin regulation. Moreover, the groundbreaking subangstrom resolution structure of a yeast aquaporin allows hydrogens to be visualized in the... (More)
Aquaporins have emerged as one of the structurally best-characterized membrane protein families, with fourteen different structures available from a diverse range of organisms. While all aquaporins share the same fold and passive mechanism for water permeation, structural details allow for differences in selectivity and modes of regulation. These details are now the emphasis of aquaporin structural biology. Recent structural studies of eukaryotic aquaporins have revealed reoccurring structural themes in both gating and trafficking, implying a limited number of structural solutions to aquaporin regulation. Moreover, the groundbreaking subangstrom resolution structure of a yeast aquaporin allows hydrogens to be visualized in the water-conducting channel, providing exclusive new insights into the proton exclusion mechanism. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Current Opinion in Structural Biology
volume
33
pages
126 - 134
publisher
Elsevier
external identifiers
  • pmid:26342685
  • wos:000365362400015
  • scopus:84941131711
ISSN
1879-033X
DOI
10.1016/j.sbi.2015.08.004
language
English
LU publication?
yes
id
1b72f86a-d0c8-49df-bfe6-70747978788d (old id 8043019)
date added to LUP
2015-10-30 13:07:35
date last changed
2017-11-12 03:05:12
@article{1b72f86a-d0c8-49df-bfe6-70747978788d,
  abstract     = {Aquaporins have emerged as one of the structurally best-characterized membrane protein families, with fourteen different structures available from a diverse range of organisms. While all aquaporins share the same fold and passive mechanism for water permeation, structural details allow for differences in selectivity and modes of regulation. These details are now the emphasis of aquaporin structural biology. Recent structural studies of eukaryotic aquaporins have revealed reoccurring structural themes in both gating and trafficking, implying a limited number of structural solutions to aquaporin regulation. Moreover, the groundbreaking subangstrom resolution structure of a yeast aquaporin allows hydrogens to be visualized in the water-conducting channel, providing exclusive new insights into the proton exclusion mechanism.},
  author       = {Kreida, Stefan and Horsefield, Susanna},
  issn         = {1879-033X},
  language     = {eng},
  pages        = {126--134},
  publisher    = {Elsevier},
  series       = {Current Opinion in Structural Biology},
  title        = {Structural insights into aquaporin selectivity and regulation.},
  url          = {http://dx.doi.org/10.1016/j.sbi.2015.08.004},
  volume       = {33},
  year         = {2015},
}