Molecular modeling of voltage-gated potassium channel pore

Zhongguo Yao Li Xue Bao. 1997 Jul;18(4):323-30.

Abstract

Aim: To build a structure model for the pore of voltage-gated Shaker potassium channel and examine its validity.

Methods: (1) Structural restraints were derived from experimental and theoretical studies; (2) An initial structural motif satisfying the derived restraints was first constructed, and further refined by restrained molecular mechanics; (3) The quality of the model was judged by the criterion that whether it could clarify molecular mechanisms of channel functions and explain the known experimental facts.

Results: (1) A computer pore structure was proposed, in which the residues within signature sequence (corresponding to Shaker 439-446) dipped into the membrane and formed the narrow part of the pore in a non-periodic conformation, while the other residues in the P region constituted the outer mouth of the pore; (2) The ion selectivity was achieved through cation-pi orbital interaction mechanism at position 445 and oxygen cage mechanism at position 447; (3) Different binding modes led to different affinity of CTX and AgTx2 to channel; and (4) The inside of pore was dominated by negative electrostatic potential.

Conclusion: The model proposed was consistent with the derived restraints from the experimental results.

MeSH terms

  • Amino Acid Sequence
  • Charybdotoxin
  • Drug Interactions
  • Models, Molecular
  • Molecular Sequence Data
  • Potassium Channels / chemistry*
  • Scorpion Venoms
  • Sequence Alignment
  • Shaker Superfamily of Potassium Channels

Substances

  • Potassium Channels
  • Scorpion Venoms
  • Shaker Superfamily of Potassium Channels
  • Charybdotoxin
  • agitoxin 2