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

FIGURE 1.

FIGURE 1.

Overall structure of CCM3 in complex with paxillin LD motifs. A, a schematic diagram shows one CCM3 dimer in complex with paxillin LD4 motif. For one monomer of CCM3 the molecular surface is shown; for the other, α-helices are shown in green as cylinders and labeled. The bound LD4 motif is colored salmon. The open and closed ends of the CCM3 FAT homology domain and the N and C termini of CCM3 are indicated. B, shown is a close-up of LD4 motif binding to CCM3 FAT homology domain. The surface of CCM3 is colored by conservation as per Li et al. (11). Dark blue indicates complete conservation, gray indicates poor conservation. LD motifs bind CCM3 in the extremely well conserved HP1 site. Paxillin LD4 is colored salmon. C, structure-based sequence alignment of the CCM3 FAT homology domain with the FAT domains of FAK and Pyk2 is shown. Pyk2 residues 868–1009 (SwissProt Q14289), FAK residues 912–1052 (SwissProt Q05397), and CCM3 residues, 98–212 (SwissProt Q9BUL8) are shown. Green or yellow boxes indicate the extent of α-helices. CCM3 residues that contact LD motifs are shown in red. CCM3 residues discussed, Ala-135 and Lys-172, are boxed in red. Residue numbers for each protein are indicated. All structural figures made using CCM4MG (41).