7ynk
From Proteopedia
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[https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Familial renal glucosuria. The disease is caused by variants affecting the gene represented in this entry. | [https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Familial renal glucosuria. The disease is caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Electrogenic Na(+)-coupled sugar | + | [https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:28592437, PubMed:34880493). Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity).[UniProtKB:Q923I7]<ref>PMID:20980548</ref> <ref>PMID:28592437</ref> <ref>PMID:34880493</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sodium-Glucose Cotransporters (SGLT) mediate the uphill uptake of extracellular sugars and play fundamental roles in sugar metabolism. Although their structures in inward-open and outward-open conformations are emerging from structural studies, the trajectory of how SGLTs transit from the outward-facing to the inward-facing conformation remains unknown. Here, we present the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound state. Both structures show an occluded conformation, with not only the extracellular gate but also the intracellular gate tightly sealed. The sugar substrate are caged inside a cavity surrounded by TM1, TM2, TM3, TM6, TM7, and TM10. Further structural analysis reveals the conformational changes associated with the binding and release of substrates. These structures fill a gap in our understanding of the structural mechanisms of SGLT transporters. | ||
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| + | Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.,Cui W, Niu Y, Sun Z, Liu R, Chen L Nat Commun. 2023 May 22;14(1):2920. doi: 10.1038/s41467-023-38720-1. PMID:37217492<ref>PMID:37217492</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ynk" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Sodium/glucose cotransporter 3D structures|Sodium/glucose cotransporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of human SGLT2-MAP17 complex in the apo state in the inward-facing conformation
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