Signal transduction is an essential process in cells. One critical signaling molecule, protein kinase A (PKA), phosphorylates target proteins, thereby changing their conformations and modifying their functions. PKA is a component of multiple signaling pathways that regulate a variety of proteins. Since the broad substrate specificity of PKA can lead to phosphorylation of unintended proteins, PKA activity must be limited to specific times and places. A‐kinase anchoring proteins (AKAPs) bind and help localize PKA to specific areas. The RIIa domain in PKA provides a shallow groove for an amphipathic helix of AKAP to bind via interactions of hydrophobic side chains. A similar binding motif is found in the DPY‐30 domain, which suggests this domain may also play a localization role. The ability of AKAP to interact with PKA and regulate its activity is essential for the specificity of many cellular responses. The ability of a cell to localize proteins containing a DPY‐30 domain may also be important for proper function. If localization is disrupted, serious problems like heart disease and cancer may result. To further understand the impact of structural interactions on localization, physical models of RIIa, DPY‐30, and AKAP amphipathic helix have been designed and built by the Cedarburg High School SMART (Students Modeling a Research Topic) Team using 3D printing technology. Supported by a grant from NIH‐NCRR‐SEPA.
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