Table 1

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

Proteins

Hill

Adair

present model

Reference


PhK5

KD1 = 0.24, KD2 = 13

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

[33]

skMLCK

KD1 = 0.02, KD2 = 0.08

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

sk-N11

KD1 = 0.26, KD2 = 6

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

sk-C10

KD1 = 3.4, KD2 = 4

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

CaATPase

KD1 = 0.09, KD2 = 0.2

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

ATPase-N18

KD1 = 0.12, KD2 = 3.9

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

ATPase-C17

KD1 = 0.66, KD2 = 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


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.

Valeyev et al. BMC Systems Biology 2008 2:48   doi:10.1186/1752-0509-2-48

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