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-Structure paper
Title | Two-dimensional crystal structure of aquaporin-4 bound to the inhibitor acetazolamide. |
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Journal, issue, pages | Microscopy (Oxf), Vol. 65, Issue 2, Page 177-184, Year 2016 |
Publish date | Dec 17, 2015 |
![]() | Akiko Kamegawa / Yoko Hiroaki / Kazutoshi Tani / Yoshinori Fujiyoshi / ![]() |
PubMed Abstract | Acetazolamide (AZA) reduces the water permeability of aquaporin-4, the predominant water channel in the brain. We determined the structure of aquaporin-4 in the presence of AZA using electron ...Acetazolamide (AZA) reduces the water permeability of aquaporin-4, the predominant water channel in the brain. We determined the structure of aquaporin-4 in the presence of AZA using electron crystallography. Most of the features of the 5-Å density map were consistent with those of the previously determined atomic model. The map showed a protruding density from near the extracellular pore entrance, which most likely represents the bound AZA. Molecular docking simulations supported the location of the protrusion as the likely AZA-binding site. These findings suggest that AZA reduces water conduction by obstructing the pathway at the extracellular entrance without inducing a large conformational change in the protein. |
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Methods | EM (electron crystallography) |
Resolution | 5.0 Å |
Structure data | ![]() EMDB-3214: |
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