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3.3 angstrom structure of mouse TRPM7 with EDTA
Structural highlights
FunctionTRPM7_MOUSE Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).[1] Publication Abstract from PubMedThe transient receptor potential ion channel subfamily M, member 7 (TRPM7), is a ubiquitously expressed protein that is required for mouse embryonic development. TRPM7 contains both an ion channel and an alpha-kinase. The channel domain comprises a nonselective cation channel with notable permeability to Mg(2+) and Zn(2+) Here, we report the closed state structures of the mouse TRPM7 channel domain in three different ionic conditions to overall resolutions of 3.3, 3.7, and 4.1 A. The structures reveal key residues for an ion binding site in the selectivity filter, with proposed partially hydrated Mg(2+) ions occupying the center of the conduction pore. In high [Mg(2+)], a prominent external disulfide bond is found in the pore helix, which is essential for ion channel function. Our results provide a structural framework for understanding the TRPM1/3/6/7 subfamily and extend the knowledge base upon which to study the diversity and evolution of TRP channels. Structure of the mammalian TRPM7, a magnesium channel required during embryonic development.,Duan J, Li Z, Li J, Hulse RE, Santa-Cruz A, Valinsky WC, Abiria SA, Krapivinsky G, Zhang J, Clapham DE Proc Natl Acad Sci U S A. 2018 Aug 14. pii: 1810719115. doi:, 10.1073/pnas.1810719115. PMID:30108148[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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