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TitleImplications of the aquaporin-4 structure on array formation and cell adhesion.
Journal, issue, pagesJ Mol Biol, Vol. 355, Issue 4, Page 628-639, Year 2006
Publish dateJan 27, 2006
AuthorsYoko Hiroaki / Kazutoshi Tani / Akiko Kamegawa / Nobuhiko Gyobu / Kouki Nishikawa / Hiroshi Suzuki / Thomas Walz / Sei Sasaki / Kaoru Mitsuoka / Kazushi Kimura / Akira Mizoguchi / Yoshinori Fujiyoshi /
PubMed AbstractAquaporin-4 (AQP4) is the predominant water channel in the mammalian brain and an important drug target for treatment of cerebral edema, bipolar disorder and mesial temporal lobe epilepsy. We ...Aquaporin-4 (AQP4) is the predominant water channel in the mammalian brain and an important drug target for treatment of cerebral edema, bipolar disorder and mesial temporal lobe epilepsy. We determined the AQP4 structure by electron crystallography of double-layered, two-dimensional (2D) crystals. The structure allows us to discuss how the expression ratio between the long and short AQP4 splicing variant can determine the size of in vivo orthogonal arrays. Furthermore, AQP4 contains a short 3(10) helix in an extracellular loop, which mediates weak but specific interactions between AQP4 molecules in adjoining membranes. This finding suggests a previously unexpected role for AQP4 in cell adhesion. This notion was corroborated by expression of AQP4 in L-cells, which resulted in clustering of the cells. Our AQP4 structure thus enables us to propose models for the size regulation of orthogonal arrays and channel-mediated cell adhesion.
External linksJ Mol Biol / PubMed:16325200
MethodsEM (electron crystallography)
Resolution3.2 Å
Structure data

PDB-2d57:
Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 3.2 Å

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / WATER TRANSPORT / WATER CHANNEL / AQUAPORIN / TWO-DIMENSIONAL CRYSTAL / MEMBRANE PROTEIN / BACULOVIRUS EXPRESSION SYSTEM

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