8amx

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'''Unreleased structure'''
 
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The entry 8amx is ON HOLD until Paper Publication
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==AQP7 dimer of tetramers_D4==
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<StructureSection load='8amx' size='340' side='right'caption='[[8amx]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8amx]] is a 8 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=8AMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AMX FirstGlance]. <br>
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</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=8amx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8amx OCA], [https://pdbe.org/8amx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8amx RCSB], [https://www.ebi.ac.uk/pdbsum/8amx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8amx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AQP7_HUMAN AQP7_HUMAN] Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (PubMed:9405233, PubMed:11952783, PubMed:30423801, PubMed:30420639). The channel is also permeable to urea (PubMed:9405233). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity).[UniProtKB:O54794]<ref>PMID:11952783</ref> <ref>PMID:30420639</ref> <ref>PMID:30423801</ref> <ref>PMID:9405233</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 A resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic alpha- and beta- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.
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Authors:
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Cryo-EM structure supports a role of AQP7 as a junction protein.,Huang P, Venskutonyte R, Prasad RB, Ardalani H, de Mare SW, Fan X, Li P, Spegel P, Yan N, Gourdon P, Artner I, Lindkvist-Petersson K Nat Commun. 2023 Feb 3;14(1):600. doi: 10.1038/s41467-023-36272-y. PMID:36737436<ref>PMID:36737436</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8amx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Fan X]]
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[[Category: Gourdon P]]
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[[Category: Huang P]]
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[[Category: Li P]]
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[[Category: Lindkvist-Petersson K]]
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[[Category: Venskutonyte R]]
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[[Category: Yan N]]

Revision as of 10:26, 15 February 2023

AQP7 dimer of tetramers_D4

PDB ID 8amx

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