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  Aquaglyceroporins, one channel for two molecules

Thomas, D., Bron, P., Ranchy, G., Duchesne, L., Cavalier, A., Rolland, J. P., et al. (2002). Aquaglyceroporins, one channel for two molecules. Biochimica et Biophysica Acta: BBA, 1555(1-3), 181-186. doi:10.1016/s0005-2728(02)00275-x.

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 Creators:
Thomas, D., Author
Bron, P., Author
Ranchy, G., Author
Duchesne, L., Author
Cavalier, A., Author
Rolland, J. P., Author
Raguenes-Nicol, C., Author
Hubert, J. F., Author
Haase, W.1, 2, Author              
Delamarche, C., Author
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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Free keywords: Animal ; *Aquaporins/ch [Chemistry] ; Bacterial Proteins/bi [Biosynthesis] ; *Bacterial Proteins/ch [Chemistry] ; Bacterial Proteins/ge [Genetics] ; Binding Sites ; Cell Membrane/me [Metabolism] ; Cell Membrane/ul [Ultrastructure] ; Comparative Study ; Escherichia coli Proteins/ch [Chemistry] ; Freeze Fracturing ; Glycerol/ch [Chemistry] ; *Lactococcus lactis/ch [Chemistry] ; Lactococcus lactis/ge [Genetics] ; Microscopy, Electron ; Models, Molecular ; Oocytes/me [Metabolism] ; Particle Size ; Water/ch [Chemistry] ; Xenopus
 Abstract: In the light of the recently published structure of GlpF and AQP1, we have analysed the nature of the residues which could be involved in the formation of the selectivity filter of aquaporins, glycerol facilitators and aquaglyceroporins. We demonstrate that the functional specificity for major intrinsic protein (MIP) channels can be explained on one side by analysing the polar environment of the residues that form the selective filter. On the other side, we show that the channel selectivity could be associated with the oligomeric state of the membrane protein. We conclude that a non-polar environment in the vicinity of the top of helix 5 could allow aquaglyceroporins and GlpF to exist as monomers within the hydrophobic environment of the membrane.

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Language(s): eng - English
 Dates: 2002-05-292002-04-222002-05-292002-06-262002
 Publication Status: Published in print
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 12091
DOI: 10.1016/s0005-2728(02)00275-x
 Degree: -

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Title: Biochimica et Biophysica Acta : BBA
  Other : Biochimica et Biophysica Acta (BBA) - Biomembranes
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1555 (1-3) Sequence Number: - Start / End Page: 181 - 186 Identifier: Other: 1879-2642
CoNE: https://pure.mpg.de/cone/journals/resource/18792642