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Dynamics of crucial protein 'switch' revealed
Date:5/17/2011

especially good at studying the structural motion of proteins.

Using this novel approach, the investigators were able to reveal, in fine detail, that cAMP interacts with its two known binding sites on Epac2 in a sequential fashion and that binding of cAMP changes the shape of the protein in a very specific way switching on its activity by exposing further signaling interaction sites on Epac2.

"DXMS analysis has proved to be an amazingly powerful approach, alone or in combination with other techniques, in figuring out how proteins work as molecular machines, changing their shapes or morphing in the normal course of their function," said Woods. "This will be of great use in the identification and development of therapeutic drugs that target these protein motions."


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Contact: Molly Dannenmaier
mjdannen@utmb.edu
409-772-8790
University of Texas Medical Branch at Galveston
Source:Eurekalert

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