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• W2043586697 abstract "Calsequestrin, the major calcium storage protein in both cardiac and skeletal muscle, binds large amounts of Ca(2+) in the sarcoplasmic reticulum and releases them during muscle contraction. For the first time, the crystal structures of Ca(2+) complexes for both human (hCASQ1) and rabbit (rCASQ1) skeletal calsequestrin were determined, clearly defining their Ca(2+) sequestration capabilities through resolution of high- and low-affinity Ca(2+)-binding sites. rCASQ1 crystallized in low CaCl(2) buffer reveals three high-affinity Ca(2+) sites with trigonal bipyramidal, octahedral, and pentagonal bipyramidal coordination geometries, along with three low-affinity Ca(2+) sites. hCASQ1 crystallized in high CaCl(2) shows 15 Ca(2+) ions, including the six Ca(2+) ions in rCASQ1. Most of the low-affinity sites, some of which are μ-carboxylate-bridged, are established by the rotation of dimer interfaces, indicating cooperative Ca(2+) binding that is consistent with our atomic absorption spectroscopic data. On the basis of these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca(2+)-binding activity of calsequestrin." @default.
• W2043586697 created "2016-06-24" @default.
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• W2043586697 date "2012-03-01" @default.
• W2043586697 modified "2023-10-17" @default.
• W2043586697 title "High-capacity Ca2+ Binding of Human Skeletal Calsequestrin" @default.
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• W2043586697 doi "https://doi.org/10.1074/jbc.m111.335075" @default.
• W2043586697 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3322862" @default.
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