Sandbox Reserved 1601: Difference between revisions

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===Selectivity Filter===

The selectivity filter of the MCU is composed by many acidic amino acids near the narrow mouth of the channel which leads to high affinity for calcium (dissociation constant of less than 2nM).<ref name="Baradaran"/> The arrangement of the highly conserved WDXXEP motif in the TM2 helices form a ring in the pore to which calcium ions are attracted.<ref name="Baradaran"/> The structure in the animation is the MCU of ''Cyphellophora europaea'' so every amino acid named here specifically is that of ''C. europaea'', but most of these residues are highly conserved across all species, though residue number may change. Though not part of the WDXXEP motif, Asp221 is present at the mouth of the MCU and serves to congregate positively charged calcium ions at the entrance of the channel.<ref name="Baradaran"/> The WDXXEP motif consists of Trp224 at the N-terminal end, Asp225, Glu228, and Pro229.<ref name="Baradaran"/> Trp224 and Pro229 pack against each other and are oriented towards the pore, but only serve to stabilize Asp225 and Glu228, not interact with calcium ions.<ref name="Baradaran"/><ref name="Fan"/> The X residues (Val226 and Met227 in this case) face away from the pore and are exposed to the membrane.<ref name="Baradaran"/> The negatively charged side chains of Asp225 and Glu228 point towards the pore and form rings of radius 2.5Å and 1Å, respectively.<ref name="Baradaran"/> It's a combination of these radii and charges that account for the selectivity of the MCU. For example, potassium has an ionic radius of 1.38Å which is much larger than the 1.00Å ionic radius of calcium.<ref name="Baradaran"/> Additionally, even though sodium ions have a similar ionic radius, the +2 charge on calcium is better matched to coordination with the glutamate residues.<ref name="Baradaran"/>

===Movement of Calcium===

Sandbox Reserved 1601: Difference between revisions

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 ===Selectivity Filter===
+The selectivity filter of the MCU is composed by many acidic amino acids near the narrow mouth of the channel which leads to high affinity for calcium (dissociation constant of less than 2nM).<ref name="Baradaran"/> The arrangement of the highly conserved WDXXEP motif in the TM2 helices form a ring in the pore to which calcium ions are attracted.<ref name="Baradaran"/> The structure in the animation is the MCU of ''Cyphellophora europaea'' so every amino acid named here specifically is that of ''C. europaea'', but most of these residues are highly conserved across all species, though residue number may change. Though not part of the WDXXEP motif, Asp221 is present at the mouth of the MCU and serves to congregate positively charged calcium ions at the entrance of the channel.<ref name="Baradaran"/> The WDXXEP motif consists of Trp224 at the N-terminal end, Asp225, Glu228, and Pro229.<ref name="Baradaran"/> Trp224 and Pro229 pack against each other and are oriented towards the pore, but only serve to stabilize Asp225 and Glu228, not interact with calcium ions.<ref name="Baradaran"/><ref name="Fan"/> The X residues (Val226 and Met227 in this case) face away from the pore and are exposed to the membrane.<ref name="Baradaran"/> The negatively charged side chains of Asp225 and Glu228 point towards the pore and form rings of radius 2.5Å and 1Å, respectively.<ref name="Baradaran"/> It's a combination of these radii and charges that account for the selectivity of the MCU. For example, potassium has an ionic radius of 1.38Å which is much larger than the 1.00Å ionic radius of calcium.<ref name="Baradaran"/> Additionally, even though sodium ions have a similar ionic radius, the +2 charge on calcium is better matched to coordination with the glutamate residues.<ref name="Baradaran"/>
 ===Movement of Calcium===