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Table 1 Ca2+-CaM dissociation constants derived by the different mathematical models.

From: Elucidating the mechanisms of cooperative calcium-calmodulin interactions: a structural systems biology approach

Proteins

Hill

Adair

present model

Reference

PhK5

KD 1= 0.24, KD 2= 13

 

K1 = 1, Kc1 = 1, K2 = 1, Kc2 = 1

[33]

skMLCK

KD 1= 0.02, KD 2= 0.08

 

K1 = 0.04, Kc1 = 0.02, K2 = 0.04, Kc2 = 0.02

 

sk-N11

KD 1= 0.26, KD 2= 6

 

K1 = 1.2, K2 = 0.5 K1 = 5, K2 = 1

 

sk-C10

KD 1= 3.4, KD 2= 4

 

K1 = 0.06, Kc1 = 0.02, K2 = 0.06, Kc2 = 0.02

 

CaATPase

KD 1= 0.09, KD 2= 0.2

 

K1 = 0.15, Kc1 = 0.05, K2 = 0.15, Kc2 = 0.05

 

ATPase-N18

KD 1= 0.12, KD 2= 3.9

 

K1 = 2, Kc1 = 1, K2 = 2, Kc2 = 1

 

ATPase-C17

KD 1= 0.66, KD 2= 2.4

 

K1 = 0.4, Kc1 = 0.2 K2 = 2, Kc2 = 1

 

CaMKII-cbp

  

K1 = 0.5, Kc1 = 0.5, K2 = 0.5, Kc2 = 0.5

[49]

CaMKII

  

K1 = 5, Kc1 = 5, K2 = 5, Kc2 = 5

 

CaM pH = 7.2

 

K1 = 0.34, K2 = 0.36, K3 = 0.13, K4 = 0.06

K1 = 17, Kc1 = 7, K2 = 20, Kc2 = 0.5

[12]

F12

 

K1 = 0.142, K2 = 0.062

K1 = 17, Kc1 = 7, K2 = 17, Kc2 = 7

 

F34

 

K3 = 0.0543, K4 = 1.82

K1 = 20, Kc1 = 0.5, K2 = 20, Kc2 = 0.5

 

CaM pH = 6

  

K1 = 10, Kc1 = 5, K2 = 10, Kc2 = 5

[9]

CaM pH = 10.1

  

K1 = 2, Kc1 = 1.8, K2 = 2, Kc2 = 1.8

 
  1. K1 is the dissociation constant for a Ca2+ binding site in the N-terminal, Kc1 is a cooperatively modified dissociation constant for a Ca2+ binding site in the N-terminal when a neighbouring site is occupied, K2 is a dissociation constant for a Ca2+ binding site in the C-terminal, and Kc2 is a cooperatively influenced dissociation constant for a Ca2+ binding site in the C-terminal when a neighbouring site is occupied. All constants shown are in μM.