View source for 9qsx


==Cryo-EM structure of aquaporin 3 at pH 8.0==
<StructureSection load='9qsx' size='340' side='right'caption='[[9qsx]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9qsx]] 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=9QSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QSX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1H8K:trimethyl-[2-[oxidanyl-[3,3,4,4,5,5,6,6,7,7,8,8,8-tridecakis(fluoranyl)octoxy]phosphoryl]oxyethyl]azanium'>A1H8K</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=9qsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qsx OCA], [https://pdbe.org/9qsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qsx RCSB], [https://www.ebi.ac.uk/pdbsum/9qsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qsx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Regulation of intracellular levels of reactive oxygen species (ROS) remains poorly understood. Aquaporin 3 (AQP3) facilitates the membrane transport of hydrogen peroxide (H(2)O(2)), a key ROS signaling molecule. Here we elucidate the molecular mechanism of AQP3 and show that its regulatory properties are both pH dependent and autoregulated by H(2)O(2). Using single particle cryo-electron microscopy, we present open and closed conformations of human AQP3. At pH 8.0, the channel adopts an open state, while acidic pH or exposure to H(2)O(2) promotes closure via a large conformational rearrangement of extracellular loop E. These findings reveal a mechanism for autoregulation of H(2)O(2) transport and establish AQP3 as a key modulator of redox homeostasis in human pancreatic beta-cells.

Structural insights into AQP3 channel closure upon pH and redox changes reveal an autoregulatory molecular mechanism.,Huang P, Venskutonyte R, Wilson CJ, Bsharat S, Prasad RB, Gourdon P, Artner I, de Groot BL, Lindkvist-Petersson K Nat Commun. 2025 Dec 22;16(1):10997. doi: 10.1038/s41467-025-67144-2. PMID:41429774<ref>PMID:41429774</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9qsx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Huang P]]
[[Category: Lindkvist-Petersson K]]
[[Category: Venskutonyte R]]