7w7s
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==High resolution structure of a fish aquaporin reveals a novel extracellular fold.== | |
| + | <StructureSection load='7w7s' size='340' side='right'caption='[[7w7s]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7w7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabas_testudineus Anabas testudineus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W7S FirstGlance]. <br> | ||
| + | </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=7w7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w7s OCA], [https://pdbe.org/7w7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w7s RCSB], [https://www.ebi.ac.uk/pdbsum/7w7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w7s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/M1K561_ANATE M1K561_ANATE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aquaporins are protein channels embedded in the lipid bilayer in cells from all organisms on earth that are crucial for water homeostasis. In fish, aquaporins are believed to be important for osmoregulation; however, the molecular mechanism behind this is poorly understood. Here, we present the first structural and functional characterization of a fish aquaporin; cpAQP1aa from the fresh water fish climbing perch (<i>Anabas testudineus</i>), a species that is of high osmoregulatory interest because of its ability to spend time in seawater and on land. These studies show that cpAQP1aa is a water-specific aquaporin with a unique fold on the extracellular side that results in a constriction region. Functional analysis combined with molecular dynamic simulations suggests that phosphorylation at two sites causes structural perturbations in this region that may have implications for channel gating from the extracellular side. | ||
| - | + | High-resolution structure of a fish aquaporin reveals a novel extracellular fold.,Zeng J, Schmitz F, Isaksson S, Glas J, Arbab O, Andersson M, Sundell K, Eriksson LA, Swaminathan K, Tornroth-Horsefield S, Hedfalk K Life Sci Alliance. 2022 Oct 13;5(12):e202201491. doi: 10.26508/lsa.202201491. PMID:36229063<ref>PMID:36229063</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7w7s" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Anabas testudineus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andersson M]] | ||
| + | [[Category: Arbab O]] | ||
| + | [[Category: Eriksson L]] | ||
| + | [[Category: Glas J]] | ||
| + | [[Category: Hedfalk K]] | ||
| + | [[Category: Isaksson S]] | ||
| + | [[Category: Schmitz F]] | ||
| + | [[Category: Sundell K]] | ||
| + | [[Category: Swaminathan K]] | ||
| + | [[Category: Tornroth-Horsefield S]] | ||
| + | [[Category: Zeng J]] | ||
Revision as of 17:11, 26 April 2023
High resolution structure of a fish aquaporin reveals a novel extracellular fold.
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