Structural Study of the Complex of the Mutant Cholera Toxin A1 Subunit with Human ADP-Ribosylating Factor 6 Bound to Agmatine Chang, Shih-chia Cholera is a severe disease that causes devastating diarrhea when Vibrio cholerae infects the human intestine. Once the bacterium gets the access into the intestinal cell, adenosine diphosphate (ADP)- ribosylation of the human signaling protein Gs!!is catalyzed by the cholera toxin A1 subunit (CTA1). According to the previous researches, this reaction is activated allosterically by a GTP-bound human ADP-ribosylation factor six (ARF6). Arginine is one of the substrates for cholera toxin A1 subunit. In the thesis, the crystal structure of agmatine, a L-arginine analogue, bound to the protein complex of the mutant CTA1 with ARF6-GTP reveals the possibility of how arginine might interact with the complex. M.S. in Molecular Biochemistry and Biophysics, July 2012 Howard, Andrew J 2012-07-12 2012-07 Thesis application/pdf islandora:7038 http://hdl.handle.net/10560/2897 BIOL / Biology Illinois Institute of Technology en In Copyright http://rightsstatements.org/page/InC/1.0/ Restricted Access