View source for 1ymg


==The Channel Architecture of Aquaporin O at 2.2 Angstrom Resolution==
<StructureSection load='1ymg' size='340' side='right'caption='[[1ymg]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ymg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tm8 1tm8]. The May 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Aquaporin''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_5 10.2210/rcsb_pdb/mom_2014_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YMG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></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=1ymg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymg OCA], [https://pdbe.org/1ymg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ymg RCSB], [https://www.ebi.ac.uk/pdbsum/1ymg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ymg ProSAT]</span></td></tr>
</table>
== 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> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ym/1ymg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ymg ConSurf].
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== Publication Abstract from PubMed ==
We determined the x-ray structure of bovine aquaporin 0 (AQP0) to a resolution of 2.2 A. The structure of this eukaryotic, integral membrane protein suggests that the selectivity of AQP0 for water transport is based on the identity and location of signature amino acid residues that are hallmarks of the water-selective arm of the AQP family of proteins. Furthermore, the channel lumen is narrowed only by two, quasi-2-fold related tyrosine side chains that might account for reduced water conductance relative to other AQPs. The channel is functionally open to the passage of water because there are eight discreet water molecules within the channel. Comparison of this structure with the recent electron-diffraction structure of the junctional form of sheep AQP0 at pH 6.0 that was interpreted as closed shows no global change in the structure of AQP0 and only small changes in side-chain positions. We observed no structural change to the channel or the molecule as a whole at pH 10, which could be interpreted as the postulated pH-gating mechanism of AQP0-mediated water transport at pH &gt;6.5. Contrary to the electron-diffraction structure, the comparison shows no evidence of channel gating induced by association of the extracellular domains of AQP0 at pH 6.0. Our structure aids the analysis of the interaction of the extracellular domains and the possibility of a cell-cell adhesion role for AQP0. In addition, our structure illustrates the basis for formation of certain types of cataracts that are the result of mutations.

The channel architecture of aquaporin 0 at a 2.2-A resolution.,Harries WE, Akhavan D, Miercke LJ, Khademi S, Stroud RM Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14045-50. Epub 2004 Sep 17. PMID:15377788<ref>PMID:15377788</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1ymg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aquaporin 3D structures|Aquaporin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquaporin]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Akhavan D]]
[[Category: Harries WEC]]
[[Category: Khademi S]]
[[Category: Miercke LJW]]
[[Category: Stroud RM]]