Table 1 Biochemical analysis of CAP1 mutants

From: Structural basis of actin monomer re-charging by cyclase-associated protein

   

G-actin binding

Nucleotide exchange

 

Mutant #

 

ATP-actin

ADP-actin

 
  

Wild type

++

++++

++++

WH2 domain

1

R253A L256A I260A

+++

++

2

Δ266ITHA269

+++

+

3

270LKHV273 → 270AAAA273

+++

4

279THKN282 → 279AAAA282

+

++++

++++

CARP domain primary interface

5

K347A Y351A Y353A

++

+

+++++

6

K365A N367A D372A

++

CARP domain secondary interface

7

D446A E449A

++

+

+++++

8

Δ471EIAG474

++

+++++

++

9

Y418A F447A

++

10

L339A Q399A D446A

++

++

+++++

  1. A summary table of C-CAP mutant affinities for ADP-G-actin and ATP-G-actin, and their effects on nucleotide exchange on ADP-actin monomers (see Supplementary Figs. 3c, d, 4). Symbols: Kd for ATP-actin: ++ (0.5–2 μM), + (2–5 μM), – (unmeasurable). Kd for ADP-actin: +++++ (0.005–0.025 μM), ++++ (0.025–0.1 μM), +++ (0.1–0.3 μM), ++ (0.3–1 μM), + (>1 μM), – (unmeasurable). Half-times of nucleotide exchange: +++++ (2–8s), ++++ (8–15s), +++ (15–19s), ++ (19–24s), + (24–28s), – (>29s)