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| | ==Human Aquaporin 5 (AQP5) - High Resolution X-ray Structure== | | ==Human Aquaporin 5 (AQP5) - High Resolution X-ray Structure== |
| - | <StructureSection load='3d9s' size='340' side='right' caption='[[3d9s]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3d9s' size='340' side='right'caption='[[3d9s]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3d9s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3d9s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D9S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PS6:O-[(S)-{[(2S)-2-(HEXANOYLOXY)-3-(TETRADECANOYLOXY)PROPYL]OXY}(HYDROXY)PHOSPHORYL]-D-SERINE'>PS6</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AQP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PS6:O-[(S)-{[(2S)-2-(HEXANOYLOXY)-3-(TETRADECANOYLOXY)PROPYL]OXY}(HYDROXY)PHOSPHORYL]-D-SERINE'>PS6</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3d9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9s OCA], [http://pdbe.org/3d9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d9s RCSB], [http://www.ebi.ac.uk/pdbsum/3d9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9s ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d9s OCA], [https://pdbe.org/3d9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d9s RCSB], [https://www.ebi.ac.uk/pdbsum/3d9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d9s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AQP5_HUMAN AQP5_HUMAN]] Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions. | + | [https://www.uniprot.org/uniprot/AQP5_HUMAN AQP5_HUMAN] Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Aquaporin|Aquaporin]] | + | *[[Aquaporin 3D structures|Aquaporin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Backmark, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Fellert, M]] | + | [[Category: Backmark A]] |
| - | [[Category: Horsefield, R]] | + | [[Category: Fellert M]] |
| - | [[Category: Johanson, U]] | + | [[Category: Horsefield R]] |
| - | [[Category: Kjellbom, P]] | + | [[Category: Johanson U]] |
| - | [[Category: Kvassman, J]] | + | [[Category: Kjellbom P]] |
| - | [[Category: Neutze, R]] | + | [[Category: Kvassman J]] |
| - | [[Category: Norden, K]] | + | [[Category: Neutze R]] |
| - | [[Category: Scheltinga, A C.Terwisscha Van]] | + | [[Category: Norden K]] |
| - | [[Category: Tornroth-Horsefield, S]] | + | [[Category: Terwisscha Van Scheltinga AC]] |
| - | [[Category: Aqp]]
| + | [[Category: Tornroth-Horsefield S]] |
| - | [[Category: Aquaglyceroporin]]
| + | |
| - | [[Category: Aquaporin]]
| + | |
| - | [[Category: Ar/r]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Lipid]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Npa]]
| + | |
| - | [[Category: Phosphatidylserine]]
| + | |
| - | [[Category: Psf]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Water channel]]
| + | |
| - | [[Category: Water transport]]
| + | |
| Structural highlights
Function
AQP5_HUMAN Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human aquaporin 5 (HsAQP5) facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-A resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking.
High-resolution x-ray structure of human aquaporin 5.,Horsefield R, Norden K, Fellert M, Backmark A, Tornroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13327-32. Epub 2008 Sep 3. PMID:18768791[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Horsefield R, Norden K, Fellert M, Backmark A, Tornroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R. High-resolution x-ray structure of human aquaporin 5. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13327-32. Epub 2008 Sep 3. PMID:18768791
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