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Table 1 Amino acid residues participating in interactions of NTX-1 with receptor interface determined by docking simulation.

From: Binding of long-chain α-neurotoxin would stabilize the resting state of nAChR: A comparative study with α-conotoxin

  T.nAChR subunit interface
NTX-1 Principal site (alpha 1) Complementary site (gamma) Average occupancy during MD
Loop I    
Thr 6 Thr 191 Arg 186  
Ile 8 Pro 194, Cys 193, Cys 192, Thr 191 Ile 172 Ile8 Thr 191 (α1) 0.8
    Ile8 pro 194 (α1) 0.7
    Ile8 Cys 192 (α1) 0.9
Loop II    
TRp 31 Tyr 190, Val 188 Asp 176, Glu 175, Trp31 Val 188 (α1) 0.9
    Trp31 Tyr 190 (α1) 0.9
Cys 32   Asp 176, Thr 37 Cys32 Asp 176 (γ) 0.9
    Cys32 Glu 175 (γ) 0.9
Gly 33   Trp 54 Gly33 Asp 176 (γ) 0.9
Ser 34 Tyr 93 Leu 118, Trp 54, Ser34 Trp 54 (γ) 0.7
    Ser34 Tyr 93 (α1) 0.6
Arg 35*   Glu 175 Arg 35* Leu 118 (γ) 0.9
    Arg 35* Trp 54 (γ) 0.9
    Arg 35* Trp 149 (α) 0.9
Gly 36 Tyr 190 Gln 58  
Lys 37    Lys 37 Glu (γ) 0.8
Val 38 Thr 191   Val38 Thr 191 (α1) 0.9
Ile 39 Thr 191, Cys 192   Ile Thr 191 (α1) 0.9
Loop III    
Ser 52    
Tyr 53    Tyr53 Leu 172 (γ) 0.9
C-Tail    
Gln 70 Pro 194, Cys 193   Arg72 Cys 193 (α1) 1
Lys 71 Cys 193,   Lys71 Cys 193 (α1) 1
Arg 72 Cys 193   Gln70 Cys 193 (α1) 1
Pro 73 Cys 192, Cys 193   Gln70 Pro 194 (α1) 0.9
  1. Average occupancies of the main anchor point residues participating in interactions of NTX-1 with receptor (α/γ interface) after 7 ns molecular dynamics simulation and within 5 Å distance along the simulation trajectory.The critical residue Arg 35 at the tip of Loop II is marked with a star. Amino acids making hydrogen bonds are underlined.