5c5x

CRYSTAL STRUCTURE OF THE S156E MUTANT OF HUMAN AQUAPORIN 5

spinqualitylabelsall models 5c5x, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c5x is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: PS6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AQP5_HUMAN Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions. Publication Abstract from PubMed Aquaporin membrane protein channels mediate cellular water flow. Human aquaporin 5 (AQP5) is highly expressed in the respiratory system and secretory glands where it facilitates the osmotically-driven generation of pulmonary secretions, saliva, sweat and tears. Dysfunctional trafficking of AQP5 has been implicated in several human disease states, including Sjogren's syndrome, bronchitis and cystic fibrosis. In order to investigate how the plasma membrane expression levels of AQP5 are regulated, we studied real-time translocation of GFP-tagged AQP5 in HEK293 cells. We show that AQP5 plasma membrane abundance in transfected HEK293 cells is rapidly and reversibly regulated by at least three independent mechanisms involving phosphorylation at Ser156, protein kinase A activity and extracellular tonicity. The crystal structure of a Ser156 phosphomimetic mutant indicates that its involvement in regulating AQP5 membrane abundance is not mediated by a conformational change of the carboxy-terminus. We suggest that together these pathways regulate cellular water flow. Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.,Kitchen P, Oberg F, Sjohamn J, Hedfalk K, Bill RM, Conner AC, Conner MT, Tornroth-Horsefield S PLoS One. 2015 Nov 16;10(11):e0143027. doi: 10.1371/journal.pone.0143027., eCollection 2015. PMID:26569106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin 3D structures

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