View source for 4nef


==X-ray structure of human Aquaporin 2==
<StructureSection load='4nef' size='340' side='right'caption='[[4nef]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nef]] 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=4NEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NEF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4nef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nef OCA], [https://pdbe.org/4nef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nef RCSB], [https://www.ebi.ac.uk/pdbsum/4nef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nef ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/AQP2_HUMAN AQP2_HUMAN] Nephrogenic diabetes insipidus. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/AQP2_HUMAN AQP2_HUMAN] Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human aquaporin 2 (AQP2) is a water channel found in the kidney collecting duct, where it plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin and defective trafficking results in nephrogenic diabetes insipidus (NDI). Here we present the X-ray structure of human AQP2 at 2.75 A resolution. The C terminus of AQP2 displays multiple conformations with the C-terminal alpha-helix of one protomer interacting with the cytoplasmic surface of a symmetry-related AQP2 molecule, suggesting potential protein-protein interactions involved in cellular sorting of AQP2. Two Cd(2+)-ion binding sites are observed within the AQP2 tetramer, inducing a rearrangement of loop D, which facilitates this interaction. The locations of several NDI-causing mutations can be observed in the AQP2 structure, primarily situated within transmembrane domains and the majority of which cause misfolding and ER retention. These observations provide a framework for understanding why mutations in AQP2 cause NDI as well as structural insights into AQP2 interactions that may govern its trafficking.

X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking.,Frick A, Eriksson UK, de Mattia F, Oberg F, Hedfalk K, Neutze R, de Grip WJ, Deen PM, Tornroth-Horsefield S Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6305-10. doi:, 10.1073/pnas.1321406111. Epub 2014 Apr 14. PMID:24733887<ref>PMID:24733887</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nef" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aquaporin 3D structures|Aquaporin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Deen PMT]]
[[Category: Eriksson U]]
[[Category: Frick A]]
[[Category: Grip WD]]
[[Category: Hedfalk K]]
[[Category: Mattia FD]]
[[Category: Neutze R]]
[[Category: Oberg F]]
[[Category: Tornroth-horsefield S]]