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| | <StructureSection load='2b6o' size='340' side='right'caption='[[2b6o]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2b6o' size='340' side='right'caption='[[2b6o]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b6o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2B6O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b6o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sor|1sor]], [[2b6p|2b6p]], [[1ymg|1ymg]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2b6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6o OCA], [http://pdbe.org/2b6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b6o RCSB], [http://www.ebi.ac.uk/pdbsum/2b6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6o 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=2b6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6o OCA], [https://pdbe.org/2b6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6o RCSB], [https://www.ebi.ac.uk/pdbsum/2b6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MIP_SHEEP MIP_SHEEP]] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.<ref>PMID:15141214</ref> <ref>PMID:15351655</ref> <ref>PMID:20389283</ref> | + | [https://www.uniprot.org/uniprot/MIP_SHEEP MIP_SHEEP] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.<ref>PMID:15141214</ref> <ref>PMID:15351655</ref> <ref>PMID:20389283</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Ovis aries]] | | [[Category: Ovis aries]] |
| - | [[Category: Cheng, Y]] | + | [[Category: Cheng Y]] |
| - | [[Category: Fujiyoshi, Y]] | + | [[Category: Fujiyoshi Y]] |
| - | [[Category: Gonen, T]] | + | [[Category: Gonen T]] |
| - | [[Category: Harrison, S C]] | + | [[Category: Harrison SC]] |
| - | [[Category: Hiroaki, Y]] | + | [[Category: Hiroaki Y]] |
| - | [[Category: Sliz, P]] | + | [[Category: Sliz P]] |
| - | [[Category: Walz, T]] | + | [[Category: Walz T]] |
| - | [[Category: Aqp0]]
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| - | [[Category: Aquaporin-0 junction]]
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| - | [[Category: Closed water pore]]
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| - | [[Category: Lens mip]]
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| - | [[Category: Lipid bilayer]]
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| - | [[Category: Lipid-protein interaction]]
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| - | [[Category: Membrane]]
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| - | [[Category: Membrane protein]]
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| Structural highlights
Function
MIP_SHEEP Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.[1] [2] [3]
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
Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 A resolution structure of junctional AQP0, determined by electron crystallography of double-layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic amino and carboxy termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We were therefore able to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid-protein interactions.
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.,Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T Nature. 2005 Dec 1;438(7068):633-8. PMID:16319884[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gonen T, Sliz P, Kistler J, Cheng Y, Walz T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature. 2004 May 13;429(6988):193-7. PMID:15141214 doi:10.1038/nature02503
- ↑ Gonen T, Cheng Y, Kistler J, Walz T. Aquaporin-0 membrane junctions form upon proteolytic cleavage. J Mol Biol. 2004 Sep 24;342(4):1337-45. PMID:15351655 doi:http://dx.doi.org/10.1016/j.jmb.2004.07.076
- ↑ Hite RK, Li Z, Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 2010 May 19;29(10):1652-8. Epub 2010 Apr 13. PMID:20389283 doi:10.1038/emboj.2010.68
- ↑ Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature. 2005 Dec 1;438(7068):633-8. PMID:16319884 doi:10.1038/nature04321
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