TABLE 2.

Binding affinities of CCM3 for paxillin LD motifs measured by SPR

The affinities of CCM3 for GST fusions of paxillin LD motifs, LD1, LD2, and LD4, were determined by SPR. Control experiments were conducted using the FAK FAT domain and the quadruple lysine to glutamic acid CCM3 mutant, CCM3–4KE. Binding affinities (K_D) of CCM3 for the GST-LD fusion proteins, GST-LD1, GST-LD2, and GST-LD4, were derived from two independent SPR experiments with difference surface densities of GST-LDs. Binding affinities for the FAK FAT domain and CCM3–4KE are derived from one SPR experiment. The table shows the dissociation constant (K_D) for each interaction (±S.D.). NA, not applicable.

Paxillin LD motif	KD Values
	CCM3	CCM3–4KE	FAK FAT domain
	(μm)
LD1	17 ± 3	NA	9
LD2	39 ± 2	NA	2
LD4	23 ± 6	NA	1