Calmodulin JMU: Difference between revisions

Each end of the <scene name='71/716518/Globulardomain/1'>globular domains</scene> of CaM binds to two Calcium ions, which allows CaM to bind to a total of four Calcium ions. The conformational changes which CaM undergoes allow it to be able to bind more specifically (Figure 1). Calmodulin elicits a pathway signal transduction by activating protein kinases which can then go on to phosphorylate other proteins, or other proteins can directly bind to Calmodulin<ref>doi:  10.1128/EC.01.1.119-125.2002</ref>. This would require that the other proteins have a specific binding motif or substrate binding mechanism for Calmodulin (Figure 2). Because there are many different types of binding motifs used by other proteins to interact with Calmodulin, there are no conserved amino acid sequences for CaM binding. EF-hand motifs are a common type of calcium binding motif. These motifs can be characterized as having a helix-loop-helix pattern with 12 sequence residues. Aspartic acid, asparagine, glutamate, and serine are common residues found in this motif. By forming a loop, the motif allows calcium to bind more efficiently and securely (Figure 3). Once inside the binding site, calcium can then induce a conformational change.<ref>Lewit-Bentley, A., & Rèty S. (2000). EF-hand calcium-binding proteins. The Journal of current opinion in