Sandbox Reserved 1626: Difference between revisions
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=== Selectivity Filter === | === Selectivity Filter === | ||
The pore-forming subunit of the MCU contains 351 amino acid residues with both the N- and C-terminal domains located in the matrix of the mitochondria. The two transmembrane domains, TM1 and TM2, are connected by a solvent- exposed loop with a highly conserved DXXE motif | The pore-forming subunit of the MCU contains 351 amino acid residues with both the N- and C-terminal domains located in the matrix of the mitochondria. The two transmembrane domains, TM1 and TM2, are connected by a solvent- exposed loop with a highly conserved <scene name='83/832952/Starting_scene/2'>DXXE motif</scene> which is essential for the calcium transport, located in the upper helix of TM2. The first pore-lining residues are Asp 333 and Glu336, that are both part of the highly conserved DXXE motif connecting TM1 and TM2. Each monomer has a Glu336 whose carboxylate group points toward the pore center. The diameter of the ring is 5Å meaning that the calcium is dehydrated. Trp332 stabilizes the carboxyl groups of two neighboring Glu336 residues through hydrogen bonding. The additional interaction of Trp332 with Pro337 serves to orient Glu336 for calcium coordination. Therefore, Glu336, Trp332, and Pro337 make up the highly conserved selectivity filter. <ref name="Fan"/> | ||
=== Common Mutations === | === Common Mutations === | ||
