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| | <StructureSection load='2c32' size='340' side='right'caption='[[2c32]], [[Resolution|resolution]] 7.01Å' scene=''> | | <StructureSection load='2c32' size='340' side='right'caption='[[2c32]], [[Resolution|resolution]] 7.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C32 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C32 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ymg|1ymg]]</div></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]] 7.01Å</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=2c32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c32 OCA], [https://pdbe.org/2c32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c32 RCSB], [https://www.ebi.ac.uk/pdbsum/2c32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c32 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=2c32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c32 OCA], [https://pdbe.org/2c32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c32 RCSB], [https://www.ebi.ac.uk/pdbsum/2c32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c32 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MIP_BOVIN MIP_BOVIN]] 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:16319884</ref>
| + | [https://www.uniprot.org/uniprot/MIP_BOVIN MIP_BOVIN] 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:16319884</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Palanivelu, D V]] | + | [[Category: Palanivelu DV]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Schirmer T]] |
| - | [[Category: Eye lens]]
| + | |
| - | [[Category: Gap junction]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mixed micelle]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
MIP_BOVIN 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]
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
Aquaporin-0 (AQP0) is the major membrane protein in vertebrate eye lenses. It has been proposed that AQP0 tetramers mediate contact between membranes of adjacent lens fiber cells, which would be consistent with the extraordinarily narrow inter-cellular spacing. We have obtained 3D crystals of recombinant bovine AQP0 that diffract to 7.0 A resolution. The crystal packing was determined by molecular replacement and shows that, within the cubic lattice, AQP0 tetramers are associated head-to-head along their 4-fold axes. Oligomeric states larger than the tetramer were also observed in solution by native gel electrophoresis and analytical ultracentrifugation methods. In the crystals, there are no direct contacts between octamers, and it can thus be inferred that crystalline order is mediated solely by the detergent belts surrounding the membrane protein. Across the tetramer-tetramer interface, extracellular loops A and C interdigitate at the center and the perimeter of the octamer, respectively. The octamer structure is compared with that of the recently determined structure of truncated ovine AQP0 derived from electron diffraction of 2D crystals. Intriguingly, also in these crystals, octamers are observed, but with significantly different relative tetramer-tetramer orientations. The interactions observed in the loosely packed 3D crystals reported here may in fact represent an in vivo association mode between AQP0 tetramers from juxtaposed membranes in the eye lens.
Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals.,Palanivelu DV, Kozono DE, Engel A, Suda K, Lustig A, Agre P, Schirmer T J Mol Biol. 2006 Jan 27;355(4):605-11. Epub 2005 Nov 8. PMID:16309700[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Palanivelu DV, Kozono DE, Engel A, Suda K, Lustig A, Agre P, Schirmer T. Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals. J Mol Biol. 2006 Jan 27;355(4):605-11. Epub 2005 Nov 8. PMID:16309700 doi:10.1016/j.jmb.2005.10.032
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