AGT is a homodimeric protein, as stated earlier, and has a crystal structure of an intimate dimer. This dimer consists of a large N-terminal and a small C terminus domain; figure three shows this structure (8). It is composed of 392 amino acids in one chain in the primary structure (1). The structure is stabilized by twenty one amino acids found in the N terminus, which wrap around the outside of the other monomer (8). The N terminus is made up of three layers consisting of alternating β-α-β topology formed around a central seven-stranded β-sheet (9). The C-terminus is comprised of two layers and has a α-helical face which is exposed to the protein surface (9). The open face is composed of anti-parallel β-sheets which are packed against the edge of connecting loops of the N-terminal domain (9).