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Table 1 Analysis of the LD:vinculin-tail (Vin-T) interactions observed in the crystal structure shown in Fig. 6 with PISA [31]. (1) solvation free energy gain. (2) measure of interface specificity with P < 0.5 indicating a specific interaction and P > 0.5 suggesting a non-specific interaction, possibly due to crystal packing

From: Phospho-regulated tethering of focal adhesion kinase to vinculin links force transduction to focal adhesion signaling

Protomer 1 (Chain ID)

Protomer 2 (Chain ID)

Interface Area

2)

ΔiG

(kcal/mol)(1)

ΔiG

(P-value) (2)

Vin-T (A)

LD1 (G)

320.0

-3.0

0.541

Vin-T (C)

LD1 (H)

356.1

-2.4

0.561

Vin-T (A)

LD2 (E)

620.7

-1.7

0.670

Vin-T (C)

LD2 (F)

540.5

-3.2

0.605

Vin-T (B)

LD2 (E)

325.0

-6.0

0.161

Vin-T (D)

LD2 (F)

314.8

-5.8

0.194