Calsequestrin, locus 1SJI, is a calcium storage protein for both cardiac and skeletal muscle tissue. It is responsible for binding and releasing calcium (2+) ions. These ions make it possible for the contraction and relaxation cycle to process effectively. This protein undergoes coupled calcium binding and protein polymerization. It is related to the taxonomy, Canis Lupus Familiaris or dogs.
It is shown that two structures of skeletal and cardiac Calsequestrin are superimposable due to their subunits and front to front dimers. In other words they are overlapping one another. Thus, in comparing cardiac and skeletal muscle absorbtion shows, 80 Ca(2+) per skeletal Calsequestrin and 60 (2+) per cardiac Calsequestrin. This proposes a negative 80 and 69 net charge resulting in the C-27 terminal of the amino acid within cardiac muscle Calsequestrin to become deleted. This results in a 50% Ca (2+) binding reduction and a loss of a Ca(2+) tetramer formation. The tetramer formation is essential for biological activity and function. The Loss of tetramer formation can be linked to the loss of inefectivity of the protien and lack of phage inactivity.
http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=1SJI
www.springerlink.com/index/T73Q0X5V85HJ820Q.pdf
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