Comparisons With Transducin
Upon analyzing the amino-acid sequence of α-gustducin, it was discovered that a-gustducins and a-transducins were closely related. α-gustducin's protein sequence gives it 80% identity to both rod and cone a-transducin. Despite the structural similarities, the two proteins have very different functionalities. This is not to say the two proteins do not have similar mechanism and capabilities. Transducin removes the inhibition from cGMP Phosphodiesterase, which leads to the breakdown of cGMP. Similarly, α-gustducin binds the inhibitory units subunits of taste cell camp PDE which also causes a decrease in cAMP levels. Also, the terminal 38 amino acids of α-gustducin and α-transducin are identical. This suggests that gustducin and interact with opsin and opsin-like G-coupled receptors. Conversely, this also suggests that transducin can interact with taste receptors. The structural similarities between gustducin and transducin are so great that comparison with transducin were used to propose a model of gustducin's role and functionality in taste transduction.
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