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-Structure paper
タイトル | Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 3616, Year 2024 |
掲載日 | 2024年4月29日 |
著者 | Wenxin Hu / Alex Song / Hongjin Zheng |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:38684689 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.03 - 3.55 Å |
構造データ | EMDB-41427, PDB-8tnw: EMDB-41428, PDB-8tnx: EMDB-41429, PDB-8tny: |
化合物 | ChemComp-CL: ChemComp-OXL: ChemComp-SO4: |
由来 |
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キーワード | MEMBRANE PROTEIN / SLC26A2 / sulfate transporter / human solute carrier |