Aquaporin gating
(2006) In Current Opinion in Structural Biology 16(4). p.447-456- Abstract
- An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and... (More)
- An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and 'pinching' have emerged to describe aquaporin gating. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/394791
- author
- Hedfalk, Kristina ; Tornroth-Horsefield, Susanna LU ; Nyblom, Maria ; Johanson, Urban LU ; Kjellbom, Per LU and Neutze, Richard
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Current Opinion in Structural Biology
- volume
- 16
- issue
- 4
- pages
- 447 - 456
- publisher
- Elsevier
- external identifiers
-
- wos:000240157000004
- scopus:33746596999
- ISSN
- 1879-033X
- DOI
- 10.1016/j.sbi.2006.06.009
- language
- English
- LU publication?
- yes
- id
- d686f20c-4ed9-4748-ba77-7520219db4ec (old id 394791)
- date added to LUP
- 2016-04-01 12:28:57
- date last changed
- 2022-01-27 05:43:07
@article{d686f20c-4ed9-4748-ba77-7520219db4ec, abstract = {{An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and 'pinching' have emerged to describe aquaporin gating.}}, author = {{Hedfalk, Kristina and Tornroth-Horsefield, Susanna and Nyblom, Maria and Johanson, Urban and Kjellbom, Per and Neutze, Richard}}, issn = {{1879-033X}}, language = {{eng}}, number = {{4}}, pages = {{447--456}}, publisher = {{Elsevier}}, series = {{Current Opinion in Structural Biology}}, title = {{Aquaporin gating}}, url = {{http://dx.doi.org/10.1016/j.sbi.2006.06.009}}, doi = {{10.1016/j.sbi.2006.06.009}}, volume = {{16}}, year = {{2006}}, }