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. Author manuscript; available in PMC: 2005 Oct 15.
Published in final edited form as: J Biol Chem. 2005 May 20;280(28):26169–26176. doi: 10.1074/jbc.M502102200

Fig. 2. Average minimized structures of the wild-type hLHR, as well as of the L457(3.43)R and L457(3.43)D/D578(6.44)R active mutants.

Fig. 2

In the left-hand side of each panel, the helix bundles are shown, represented by cylinders and seen from the intracellular side in a direction perpendicular to the membrane surface. The extracellular domains are not shown. Helices 1, 2, 3, 4, 5, 6, and 7 are colored in blue, orange, green, pink, yellow, cyan, and violet, respectively, and the first, second, and third intracellular loops are colored in light green, white, and magenta, respectively. The solvent-accessible surface area computed over Arg-464(3.50), Thr-467(3.53), Ile-468(3.54), and Lys-563(6.29) is represented by dots colored according to the amino acid location. In the right-hand side of each panel, details of the interactions of the Leu-457(3.43) and Asp-578(6.44) mutants are shown. The amino acid side chains are colored according to their location.