8tnw
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2== |
| + | <StructureSection load='8tnw' size='340' side='right'caption='[[8tnw]], [[Resolution|resolution]] 3.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8tnw]] 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=8TNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TNW 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]] 3.17Å</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></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=8tnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tnw OCA], [https://pdbe.org/8tnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tnw RCSB], [https://www.ebi.ac.uk/pdbsum/8tnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tnw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/S26A2_HUMAN S26A2_HUMAN] Multiple epiphyseal dysplasia type 4;Atelosteogenesis type II;Achondrogenesis type 1B;Diastrophic dysplasia. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/S26A2_HUMAN S26A2_HUMAN] Sulfate transporter. May play a role in endochondral bone formation.<ref>PMID:7923357</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SLC26A2 is a vital solute carrier responsible for transporting essential nutritional ions, including sulfate, within the human body. Pathogenic mutations within SLC26A2 give rise to a spectrum of human diseases, ranging from lethal to mild symptoms. The molecular details regarding the versatile substrate-transporter interactions and the impact of pathogenic mutations on SLC26A2 transporter function remain unclear. Here, using cryo-electron microscopy, we determine three high-resolution structures of SLC26A2 in complexes with different substrates. These structures unveil valuable insights, including the distinct features of the homodimer assembly, the dynamic nature of substrate binding, and the potential ramifications of pathogenic mutations. This structural-functional information regarding SLC26A2 will advance our understanding of cellular sulfate transport mechanisms and provide foundations for future therapeutic development against various human diseases. | ||
| - | + | Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.,Hu W, Song A, Zheng H Nat Commun. 2024 Apr 29;15(1):3616. doi: 10.1038/s41467-024-48028-3. PMID:38684689<ref>PMID:38684689</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8tnw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hu W]] | ||
| + | [[Category: Song A]] | ||
Current revision
Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2
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