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Table 2 Amino acid residues participating in interactions of conotoxin 1XGA with the α/γ receptor interface determined by docking simulation, as well as average occupancies of the main anchor point residues participating in interactions after 7 ns molecular dynamics simulation along the trajectory.

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

 

T.nAChR subunit interface

1-XGA

Principal site (alpha 1)

Complementary site (gamma)

Average occupancy during MD

GLU 1

   

CYS 2

   

CYS 3

   

ASN 4

Thr 191, Cys 192

 

Asn4 Thr191 0.9

   

Asn4 Cys192 0.8

PRO 5

   

ALA 6

Tyr 190, Val 188

 

Ala 6 Tyr190 0.5

   

Ala 6 Val 188 0.4

CYS 7

Tyr 190

 

Cys 7 Tyr 190 0.8

GLY 8

 

Trp 54

 

ARG 9*

Trp 149, Val 91, Leu 92, Asp 99, Tyr 198

Leu 118, Trp 54, Thr 37, Asn 38

Arg9* Trp 149 0.7

   

Arg9* Leu 92 0.9

   

Arg9* Trp 54 0.9

   

Arg9* Thr 37 0.8

   

Arg9* Asn 38 0.8

HIS 10

 

Leu 118, Tyr 116, Leu 108, Arg 78

His10 Leu108 0.8

   

His10 Arg 78 0.8

TYR 11

 

Trp 54, Thr 35, Asp 176

Tyr11 Trp54 0.9

   

Tyr 11Asp 176 0.7

SER 12

 

Glu 56, Leu 118, Lys 33

Ser 12 Leu118 0.4

CYS 13

 

Tyr 116

Cys13 Tyr116 0.5

  1. The critical residue Arg 9 is marked with an asterix. Amino acids making hydrogen bonds are underlined.
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Theoretical Biology and Medical Modelling

ISSN: 1742-4682