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Table 2 Intramolecular interactions of ALG-2 in Ca2+/EF3-driven arginine switching loop

From: Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2ΔGF122) and structural roles of F122 in target recognition

  

WT

ΔGF122

 

interacting atom

MF a

Ca b

Ca c

S120

    

Hydrogen

 

Distance (Å)

N

OK116

2.8

3.2

3.1

O

NG123/121

2.8

2.8

NDd

 

NH2R125/123

ND

2.8

ND

OG

OL116

2.6

ND

ND

Y124/122

    

hydrogen

    

N

OL119

3.1

3.0

3.0

OH

NE2Q159/157

ND

ND

2.8

hydrophobic

    

CB

CL119

ND

3.9

ND

 

CD1L126/124

3.9

3.7

3.9

 

CGL126/124

ND

ND

3.7

CD1

CBF122/-

3.7

3.6

-e

 

CD1L158/156

ND

ND

4.0

CD2

CD2L158/156

3.9

ND

ND

CE1

CBF122/-

3.8

3.8

-

 

CD1F122/-

3.9

ND

-

 

CD2L158/156

3.9

ND

ND

CE2

CGL158/156

3.5

ND

ND

 

CD2L158/156

3.7

3.8

ND

CZ

CD1L158/156

ND

4.0

ND

  1. a Metal-free form of des3-20ALG-2
  2. b Ca2+-bound form of des3-20ALG-2
  3. c Ca2+-bound form of des3-23ALG-2ΔGF122
  4. d Not detected in the range of 2.6-3.2 Å for hydrogen bonding and 3.2-4.0 Å for hydrophobic interaction
  5. e Not present in des3-23 ALG-2ΔGF122