Table 1 Biochemical properties of PLS3 variants carrying OI-linked mutations

From: Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling

PLS3 construct

Tm /°C ± SE

Kd/μmol·L−1 ± SD

[PLS3]50%/μmol·L−1 ± SD

pCa50% ± SD

EGTA

Ca2+

Wild type

49.47 ± 0.72

7.41 ± 0.10

0.49 ± 0.28

2.97 ± 1.48

5.46 ± 0.14

L478P

44.93 ± 0.16

2.16 ± 0.36

n/a

n/a

n/a

N446S

46.87 ± 0.07

4.79 ± 0.56

0.58 ± 0.14

6.36 ± 2.46

6.44 ± 0.21

A253_L254insN

45.94 ± 0.95

3.77 ± 0.19

0.53 ± 0.16

2.09 ± 1.55

6.66 ± 0.17

A368D

43.38 ± 0.04

4.22 ± 0.81

0.47 ± 0.15

0.59 ± 0.09

n/a

E249_A250insI-L

41.93 ± 0.18

2.56 ± 0.46

0.10 ± 0.05

0.03 ± 0.04

n/a

  1. Tm melting temperature determined by DSF, Kd equilibrium dissociation constant of PLS3 binding to F-actin, [PLS3]50% bundling efficiency of PLS3 (concentration of PLS3 at 50% of F-actin bundled), pCa50% Ca2+ sensitivity of PLS3 (-log[Ca2+] at 50% reduction in light scattering of actin bundles), SE standard error of the mean, SD standard deviation of the mean
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