| Citation | Professor Catterall is distinguished for his work on the molecular properties of voltage-gated ion channels. He was the first to isolate sodium and calcium channel proteins and demonstrate their complex subunit composition. His adroit use of antibody mapping, photoaffinity labelling, and site-directed mutagenesis has permitted him to identify the structural correlates of voltage sensors, ion pores, and inactivation gates of these channels. Similar studies have defined the receptor sites for scorpion toxins and for pore-blocking drugs used in local anesthesia and treatment of epilepsy and cardiovascular diseases. His work has also identified the sites of channel regulation by second messenger pathways acting through protein phosphorylation and G proteins, providing a molecular view of the regulation of electrical excitability. In opening the ion channel proteins to protein chemistry and molecular analysis, his findings have given new insight into channel structure and function and are an essential prelude to the determination and understanding of their three-dimensional structures. |