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. 2011 Jun 1;286(29):26138–26147. doi: 10.1074/jbc.M110.211250

FIGURE 3.

FIGURE 3.

CCM3 binds LD motifs in an analogous manner to FAK and Pyk2 FAT domains. A, a surface diagram of the CCM3 FAT homology domain (helices αF to αI) is colored by electrostatic potential (calculated in CCP4MG). Paxillin LD4 is colored salmon. Selected residues discussed in the text are labeled. B, shown is a surface diagram of the FAK FAT domain colored by electrostatic potential. Paxillin LD4 is shown in yellow. Selected residues discussed in the text are labeled. The PDB accession code for FAK/LD4 is 1OW7 (31). C, shown is a surface diagram of the Pyk2 FAT domain colored by electrostatic potential. Paxilln LD4 is shown in cyan. Selected residues discussed in the text are labeled. The PDB accession code for Pyk2/LD4 is 3GM1 (32). D, superposition of CCM3-LD4, FAK-LD4, and Pyk2-LD4 is shown. FAT and FAT homology domains are shown as cylinders, and LD4 is in schematic format. FAK-LD4 is colored yellow, Pyk2/LD4 is colored blue, and CCM3-LD4 is colored light green and salmon. E, Cα superposition of the C-terminal 15 residues of CCM3 helix αG (salmon), FAK helix 2 (yellow), and Pyk2 helix 2 (cyan) illustrates the hinge that occurs at residues Ala-135, Gly-995FAK, and Gly-914Pyk2. Residues superposed are indicated by a black bar. The PDB accession code for FAK is 1OW6 (31) and for Pyk2 is 3GM1 (32).