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| | <StructureSection load='7ch1' size='340' side='right'caption='[[7ch1]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='7ch1' size='340' side='right'caption='[[7ch1]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7ch1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CH1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ch1]] is a 2 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=7CH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CH1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7ch1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ch1 OCA], [http://pdbe.org/7ch1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7ch1 RCSB], [http://www.ebi.ac.uk/pdbsum/7ch1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7ch1 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7ch1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ch1 OCA], [https://pdbe.org/7ch1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ch1 RCSB], [https://www.ebi.ac.uk/pdbsum/7ch1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ch1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/S26A9_HUMAN S26A9_HUMAN]] DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport (PubMed:11834742). Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion (PubMed:15800055). May prefer chloride anions and mediate uncoupled chloride anion transport in an alternate-access mechanism where a saturable binding site is alternately exposed to either one or the other side of the membrane (By similarity).[UniProtKB:Q8BU91]<ref>PMID:11834742</ref> <ref>PMID:15800055</ref> | + | [https://www.uniprot.org/uniprot/S26A9_HUMAN S26A9_HUMAN] DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport (PubMed:11834742). Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion (PubMed:15800055). May prefer chloride anions and mediate uncoupled chloride anion transport in an alternate-access mechanism where a saturable binding site is alternately exposed to either one or the other side of the membrane (By similarity).[UniProtKB:Q8BU91]<ref>PMID:11834742</ref> <ref>PMID:15800055</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The human SLC26 transporter family exhibits various transport characteristics, and family member SLC26A9 performs multiple roles, including acting as Cl(-)/HCO3 (-) exchangers, Cl(-) channels, and Na(+) transporters. Some mutations of SLC26A9 are correlated with abnormalities in respiration and digestion systems. As a potential target colocalizing with CFTR in cystic fibrosis patients, SLC26A9 is of great value in drug development. Here, we present a cryo-EM structure of the human SLC26A9 dimer at 2.6 A resolution. A segment at the C-terminal end is bound to the entry of the intracellular vestibule of the putative transport pathway, which has been proven by electrophysiological experiments to be a gating modulator. Multiple chloride and sodium ions are resolved in the high-resolution structure, identifying novel ion-binding pockets for the first time. Together, our structure takes important steps in elucidating the structural features and regulatory mechanism of SLC26A9, with potential significance in the treatment of cystic fibrosis.
| + | |
| - | | + | |
| - | Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence.,Chi X, Jin X, Chen Y, Lu X, Tu X, Li X, Zhang Y, Lei J, Huang J, Huang Z, Zhou Q, Pan X Cell Discov. 2020 Aug 10;6:55. doi: 10.1038/s41421-020-00193-7. eCollection 2020. PMID:32818062<ref>PMID:32818062</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 7ch1" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y]] | + | [[Category: Chen Y]] |
| - | [[Category: Chi, X M]] | + | [[Category: Chi XM]] |
| - | [[Category: Li, X R]] | + | [[Category: Li XR]] |
| - | [[Category: Zhang, Y Y]] | + | [[Category: Zhang YY]] |
| - | [[Category: Zhou, Q]] | + | [[Category: Zhou Q]] |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
S26A9_HUMAN DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport (PubMed:11834742). Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion (PubMed:15800055). May prefer chloride anions and mediate uncoupled chloride anion transport in an alternate-access mechanism where a saturable binding site is alternately exposed to either one or the other side of the membrane (By similarity).[UniProtKB:Q8BU91][1] [2]
References
- ↑ Lohi H, Kujala M, Makela S, Lehtonen E, Kestila M, Saarialho-Kere U, Markovich D, Kere J. Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9. J Biol Chem. 2002 Apr 19;277(16):14246-54. Epub 2002 Feb 7. PMID:11834742 doi:http://dx.doi.org/10.1074/jbc.M111802200
- ↑ Xu J, Henriksnas J, Barone S, Witte D, Shull GE, Forte JG, Holm L, Soleimani M. SLC26A9 is expressed in gastric surface epithelial cells, mediates Cl-/HCO3- exchange, and is inhibited by NH4+. Am J Physiol Cell Physiol. 2005 Aug;289(2):C493-505. Epub 2005 Mar 30. PMID:15800055 doi:http://dx.doi.org/00030.2005
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