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Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2
Structural highlights
DiseaseS26A2_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. FunctionS26A2_HUMAN Sulfate transporter. May play a role in endochondral bone formation.[1] Publication Abstract from PubMedSLC26A2 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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