Ariana Peck, a graduate student in our group recently presented her research on an important protein- Calmodulin (CaM).
Calmodulin is a calcium-binding messenger protein expressed in all eukaryotic cells. CaM transduces calcium signals by binding calcium ions and thus modifying/enabling it’s interactions with various target proteins. CaM along with calcium mediates many crucial processes such as inflammation, muscle contraction, memory, and immune response. Calcium is needed as a second messenger; calcium bound to proteins such as Calmodulin combine to act as messengers in our cells. The prevailing paradigm for Calmodulin function is that CaM plus bound calcium induces a conformational change. This results in target protein binding, in turn resulting in a cascade of cellular communication.
A few of the questions Ariana and our group are trying to answer are: How are Ca2+ dynamics so well regulated, and how do cells coordinate a response? What is the structural basis of diverse CaM target recognition? What is the mechanism of conformational change and can we find molecules (i.e. therapeutics for Cardiac Arrhythmias) that stabilize particular conformations?