Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels

@article{Frnal2004ExploringSF,
  title={Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels},
  author={Karine Fr{\'e}nal and Chenqi Xu and Nicolas Wolff and Karine Wecker and Georgina B. Gurrola and Shun Zhu and Cheng-wu Chi and Lourival Domingos Possani and Jan Tytgat and Muriel Delepierre},
  journal={Proteins: Structure},
  year={2004},
  volume={56}
}
The γ‐KTx–type scorpion toxins specific for K+ channels were found to interact with ERG channels on the turret region, while α‐KTx3.2 Agitoxin‐2 binds to the pore region of the Shaker K+ channel, and α‐KTx5.3 BmP05 binds to the intermediate region of the small‐conductance calcium‐activated K‐channel (SKCa). In order to explore the critical residues for γ‐KTx binding, we determined the NMR structure of native γ‐KTx1.1 (CnErg1), a 42 amino acid residues scorpion toxin isolated from the venom of… 

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