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. 2004 Jan 15;113(2):274–284. doi: 10.1172/JCI19874

Figure 8.

Figure 8

Model of the N-terminal pair of CBS domains (CBS1 and CBS2) from the γ2 subunit of AMPK. The picture is a view of a molecular-surface representation made using the program GRASP (Department of Biochemistry, Columbia University, New York, New York, USA) (51), with CBS1 on the left. The model was made using MODELLER 6 (Department of Biopharmaceutical Sciences, University of California San Francisco, San Francisco, California, USA) (52) and was based on the atomic coordinates of the CBS domain pair from a bacterial IMPDH (Protein Data Bank code 1ZFJ) (34). Electrostatic potential at the surface is depicted as red for negative and blue for positive. The approximate positions of residues mutated in WPWS are shown. R302 and H383 occupy equivalent positions in CBS1 and CBS2, respectively, and are adjacent to each other in the model. Part of residue T400 projects into the hydrophobic cleft between the two domains.