8gve
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8gve]] 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=8GVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GVE FirstGlance]. <br> | <table><tr><td colspan='2'>[[8gve]] 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=8GVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GVE 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=8gve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gve OCA], [https://pdbe.org/8gve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gve RCSB], [https://www.ebi.ac.uk/pdbsum/8gve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gve ProSAT]</span></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]] 3.17Å</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=8gve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gve OCA], [https://pdbe.org/8gve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gve RCSB], [https://www.ebi.ac.uk/pdbsum/8gve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gve ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/B3A2_HUMAN B3A2_HUMAN] The disease may be caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/B3A2_HUMAN B3A2_HUMAN] Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity).[UniProtKB:P13808]<ref>PMID:15184086</ref> <ref>PMID:34668226</ref> | [https://www.uniprot.org/uniprot/B3A2_HUMAN B3A2_HUMAN] Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane (PubMed:15184086, PubMed:34668226). Plays an important role in osteoclast differentiation and function (PubMed:34668226). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity).[UniProtKB:P13808]<ref>PMID:15184086</ref> <ref>PMID:34668226</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The cell maintains its intracellular pH in a narrow physiological range and disrupting the pH-homeostasis could cause dysfunctional metabolic states. Anion exchanger 2 (AE2) works at high cellular pH to catalyze the exchange between the intracellular HCO(3)(-) and extracellular Cl(-), thereby maintaining the pH-homeostasis. Here, we determine the cryo-EM structures of human AE2 in five major operating states and one transitional hybrid state. Among those states, the AE2 shows the inward-facing, outward-facing, and intermediate conformations, as well as the substrate-binding pockets at two sides of the cell membrane. Furthermore, critical structural features were identified showing an interlock mechanism for interactions among the cytoplasmic N-terminal domain and the transmembrane domain and the self-inhibitory effect of the C-terminal loop. The structural and cell-based functional assay collectively demonstrate the dynamic process of the anion exchange across membranes and provide the structural basis for the pH-sensitive pH-rebalancing activity of AE2. | ||
| - | + | ==See Also== | |
| - | + | *[[Anion exchange protein 3D structures|Anion exchange protein 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
The asymmetry structure of hAE2
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Categories: Homo sapiens | Large Structures | Cao Y | Hu K | Jian L | Rao B | Xia Y | Yao D | Zhang Q
