Sandbox Reserved 820
From Proteopedia
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<Structure load='2vaf' size='500' frame='true' align='right' caption='Crystal Structure of Human Cardiac Calsequestrin, (PDB code [[2vaf]]) ' scene='56/568018/General_structure/4'/> | <Structure load='2vaf' size='500' frame='true' align='right' caption='Crystal Structure of Human Cardiac Calsequestrin, (PDB code [[2vaf]]) ' scene='56/568018/General_structure/4'/> | ||
| - | '''Calsequestrin-2''' (or '''CASQ2''') is the soluble | + | '''Calsequestrin-2''' (or '''CASQ2''') is the soluble Ca<sup>2+</sup> binding protein in the sarcoplasmic reticulum lumen of the cardiac muscle cells. CASQ2 could be either in a monomeric, homodimeric, or homooligomeric chain form depending on its bounds with Ca<sup>2+</sup>. Mutations of CASQ2 are involved in cardiac diseases such as Catecholaminergic Polymorphic Ventricular Tachycardia. |
[[Image:LoadBinary 004.gif|300px|left|thumb|Calsequestrin in the calcium cycle of myocyte contraction]] | [[Image:LoadBinary 004.gif|300px|left|thumb|Calsequestrin in the calcium cycle of myocyte contraction]] | ||
Revision as of 13:24, 29 December 2013
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Calsequestrin-2 (or CASQ2) is the soluble Ca2+ binding protein in the sarcoplasmic reticulum lumen of the cardiac muscle cells. CASQ2 could be either in a monomeric, homodimeric, or homooligomeric chain form depending on its bounds with Ca2+. Mutations of CASQ2 are involved in cardiac diseases such as Catecholaminergic Polymorphic Ventricular Tachycardia.
General Structure
There are and . can bind the Ca2+ especially the and the .
