Sandbox Reserved 820: Difference between revisions

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== Calcium Binding ==

Each monomere of CASQ2 can bind between 18 to 50 Ca2+. The Ca2+ ions bind to two or more acidic amino acids like <scene name='56/568018/Glu/2'>Glutamate</scene> or <scene name='56/568018/Asp/3'>Aspartate</scene>. These amino acids are mainly outside the CASQ2 or in the C-terminal region. It had been shown that Ca2+ binds to an Asp-rich region on the C-terminal domain. When CASQ2 form homooligomers, Ca2+ can bind in the electronegative pocket due to the front-to-front form and back-to-back form.<ref name="The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000)">http://www.sciencedirect.com/science/article/pii/S0014579300022468</ref>

Each monomere of CASQ2 can bind between 18 to 50 Ca2+. The Ca2+ ions bind to two or more acidic amino acids like <scene name='56/568018/Glu/2'>Glutamate</scene> or <scene name='56/568018/Asp/3'>Aspartate</scene>. These amino acids are mainly outside the CASQ2 or in the C-terminal region. It had been shown that Ca2+ binds to an Asp-rich region on the C-terminal domain. When CASQ2 form homooligomers, Ca2+ can bind in the electronegative pocket due to the front-to-front form and back-to-back form.<ref name="The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000)">The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000) http://www.sciencedirect.com/science/article/pii/S0014579300022468</ref>

Ca2+ is not the only ion which can bind to the CASQ2. One of them is Mg2+. The affinity is for Mg2+ is lower than the affinity for Ca2+ however the number of Ca2+ decrease. Another ion is H+. When the pH is low, more H+ will bind to the acidic amino acids and they can not bind Ca2+ anymore.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">PMID:15050380</ref>

Sandbox Reserved 820: Difference between revisions

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 == Calcium Binding ==
-Each monomere of CASQ2 can bind between 18 to 50 Ca2+. The Ca2+ ions bind to two or more acidic amino acids like <scene name='56/568018/Glu/2'>Glutamate</scene> or <scene name='56/568018/Asp/3'>Aspartate</scene>. These amino acids are mainly outside the CASQ2 or in the C-terminal region. It had been shown that Ca2+ binds to an Asp-rich region on the C-terminal domain. <!-- METTRE DU VERT MAIS LE CT N'EST PAS DISPONIBLE cf: http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2VAF&bionumber=1 -->When CASQ2 form homooligomers, Ca2+ can bind in the electronegative pocket due to the front-to-front form and back-to-back form.<ref name="The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000)">http://www.sciencedirect.com/science/article/pii/S0014579300022468</ref>
+Each monomere of CASQ2 can bind between 18 to 50 Ca2+. The Ca2+ ions bind to two or more acidic amino acids like <scene name='56/568018/Glu/2'>Glutamate</scene> or <scene name='56/568018/Asp/3'>Aspartate</scene>. These amino acids are mainly outside the CASQ2 or in the C-terminal region. It had been shown that Ca2+ binds to an Asp-rich region on the C-terminal domain. <!-- METTRE DU VERT MAIS LE CT N'EST PAS DISPONIBLE cf: http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2VAF&bionumber=1 -->When CASQ2 form homooligomers, Ca2+ can bind in the electronegative pocket due to the front-to-front form and back-to-back form.<ref name="The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000)">The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+ and interacts with triadin (Shin et al., 2000) http://www.sciencedirect.com/science/article/pii/S0014579300022468</ref>
 Ca2+ is not the only ion which can bind to the CASQ2. One of them is Mg2+. The affinity is for Mg2+ is lower than the affinity for Ca2+ however the number of Ca2+ decrease. Another ion is H+. When the pH is low, more H+ will bind to the acidic amino acids and they can not bind Ca2+ anymore.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">PMID:15050380</ref>