Protein Structure Revealed by Mass Spectrometry Technique

An advanced mass spectroscopy technique was used to detail the structure of a signaling protein critical to physiological processes involved in major diseases such as diabetes and cancer.

The protein, Epac2 (exchange protein directly activated by cAMP 2), is a guanine nucleotide exchange factor that regulates a wide variety of intracellular processes in response to second messenger cAMP (cyclic adenosine monophosphate).

A collaborative project was carried out by investigators at the University of Texas Medical Branch (Galveston, USA) and the University of California, San Diego (USA) to define the three-dimensional structure of Epac2 in the presence and absence of cAMP using an advanced mass spectroscopy technique known as hydrogen/deuterium exchange mass spectrometry (DXMS).

Results published in the May 20, 2011, issue of the Journal of Biological Chemistry revealed that that cAMP interacted with its two known binding sites on Epac2 in a sequential fashion and that binding of cAMP changed the shape of the protein in a very specific way. More...