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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gorraitz, Edurne Wright, Ernest M. Hirayama, Bruce A. Loo, Donald D. F. Jiang, Xuan |
| Description | Author Affiliation: Loo DD ( Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095-1751.); |
| Abstract | Sodium cotransporters from several different gene families belong to the leucine transporter (LeuT) structural family. Although the identification of $Na^{+}$ in binding sites is beyond the resolution of the structures, two $Na^{+}$ binding sites (Na1 and Na2) have been proposed in LeuT. Na2 is conserved in the LeuT family but Na1 is not. A biophysical method has been used to measure sodium dissociation constants $(K_{d})$ of wild-type and mutant human sodium glucose cotransport (hSGLT1) proteins to identify the $Na^{+}$ binding sites in hSGLT1. The Na1 site is formed by residues in the sugar binding pocket, and their mutation influences sodium binding to Na1 but not to Na2. For the canonical Na2 site formed by two –OH side chains, S392 and S393, and three backbone carbonyls, mutation of S392 to cysteine increased the sodium $K_{d}$ by sixfold. This was accompanied by a dramatic reduction in the apparent sugar and phlorizin affinities. We suggest that mutation of S392 in the Na2 site produces a structural rearrangement of the sugar binding pocket to disrupt both the binding of the second $Na^{+}$ and the binding of sugar. In contrast, the S393 mutations produce no significant changes in sodium, sugar, and phlorizin affinities. We conclude that the Na2 site is conserved in hSGLT1, the side chain of S392 and the backbone carbonyl of S393 are important in the first $Na^{+}$ binding, and that $Na^{+}$ binding to Na2 promotes binding to Na1 and also sugar binding. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 47 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Binding Sites Genetics Models, Biological Models, Molecular Protein Conformation Sodium-Glucose Transporter 1 Metabolism Sodium Biophysics Mutagenesis, Site-Directed Oocytes Patch-Clamp Techniques Protein Binding Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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