AI Article Synopsis
- Cystathionine- -synthase (CBS)-pair domain transporters (CNNMs) are important for regulating magnesium levels in the body by transporting magnesium ions and affecting a specific ion channel (TRPM7).
- The study presents the crystal structure of the extracellular part of tapeworm CNNM4, revealing it forms a dimer with specific molecular structures and sites for sugar molecules.
- Mutations in the extracellular domain of human CNNM4 hinder its dimerization, and a similar mutation in mouse CNNM2 negatively affects its ability to transport magnesium in cells.
Article Abstract
Cystathionine- -synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They mediate magnesium homeostasis directly by transport of Mg ions and indirectly by regulation of the transient receptor potential ion channel subfamily M member 7 (TRPM7). Here, we report the crystal structure of the extracellular domain of tapeworm CNNM4. The domain forms a dimer of immunoglobulin-like (Ig-like) folds with electron density observed for three glycosylation sites. Analytical ultracentrifugation confirms that mutations in the extracellular domain of human CNNM4 prevent its dimerization. An analogous mutation in mouse CNNM2 impairs its activity in a cellular assay of Mg transport.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10804811 | PMC |
| http://dx.doi.org/10.1002/pro.4860 | DOI Listing |
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