Skip to main content

Table 4 Significant differences in the structures of nesfatin-3s in relation to the structures of Nucb2s

From: Nesfatin-3 possesses divalent metal ion binding properties, which remain hidden in the nucleobindin-2 precursor protein

Analyzed feature

ggNesfatin-3

hsNesfatin-3

ggNucb2

hsNucb2

α-helix-to-random coil ratio for apo-protein

1

1.2

1.7

2.8

α-helix-to-random coil ratio in the presence of:

 Mg2+

1.3

1.5

1.6

3.1

 Ca2+

1.7

2.6

2.2

2.7

 Zn2+

1

1.6

0.4

3.7

Sensitivity of the apo-protein to the proteolytic hydrolysis

moderate

low

high

moderate

Sensitivity of the holo-protein (compared to the apo-protein) to the proteolytic hydrolysis in the presence of:

 Mg2+

 → 

 → 

 Ca2+

 Zn2+

Dimer-to-monomer ratio for the apo-protein at the highest used protein concentration

3:1

dimer only

monomer only

dimer only

Dimer-to-monomer ratio for the holo-protein at the highest used protein concentration and in the presence of:

 Mg2+

9:1

dimer only

1:12

9:1

 Ca2+

3:1

24:1

1:3

dimer only

 Zn2+

3:1–9:1

dimer only

mix

6:1

The Kd values estimated after the binding of:

 Mg2+

2.4 µM

n.d

230 µM

203.2 µM

 Ca2+

116.3 µM/45.9 µM

8.79 µM

190 µM/73 µM

16.8 µM/19.8 µM

 Zn2+

7.21 nM/0.4 µM/31.1 µM

6.95 µM

188 µM/34.4 µM

23.9 µM/14.3 µM

  1. The data presented for ggNucb2 and hsNucb2 were adopted from [16, 17]. Arrows indicate the stimulatory (↑), suppressive (↓), or neglected ( →) effects listed in the left column; mix – many different oligomeric forms; n.d. – not determined