MAGI1 (6th domain)
MAGI1 (6th domain): Human membrane associated guanylate kinase, WW and PDZ domain containing 1 (6th domain)
PDB Code: 3BPU
PDZ domains function as protein-protein interaction modules. The best characterised interaction of the PDZ domain is with the C-terminal 4-5 residues of the target protein that binds in an extended fashion between the betaB strand and the alphaB helix of the PDZ domain. In many cases the protein that contains the PDZ domain also possesses additional PDZ domains or interaction modules. MAGI1 is one such protein that contains a guanylate kinase domain, WW domains and five PDZ domains within its sequence.
MAGI1 is one of the components of the closely associated areas between cells that form tight junctions. It along with the small GTPase Rap1 plays a critical role in adherens junction maturation and development of the central nervous system through delta-notch signaling at adherens junctions. It also has an important role to play in apoptosis which involves the break down of cell-cell tight juctions by the cleavage of MAGI1 by the proteases caspases-3 and -7.
Here we present the crystal structure of the sixth PDZ domain of MAGI1 bound to a C-terminal peptide derived from beta-catenin. Based on homology modelling it was noted that the side chain for Cys1190 in the 6th PDZ domain of MAGI1 was likely to be exposed to solvent. In order to prevent poor biochemical behaviour this side chain was mutated into a Ser residue.
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