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Today, "Nature" published an online paper by Professor Yan Ning's team, revealing the structure of the powerful painkiller ziconotide when combined with the human N-type voltage-gated calcium channel Cav2.
▲Professor Yan Ning is the corresponding author of the study, and Gao Shuai and Dr.
The Cav2.
▲Ziconotide is derived from a toxin found in the sea snail (Conus magus) (Image source: Richard Parker, CC BY 2.
In order to better understand the mechanism of action of ziconotide, the structure when it binds to the Cav2.
It has been found that ziconotide can selectively inhibit Cav2.
▲The structure of Cav2.
Further research found that among the 8 residues that promote the binding of ziconotide, 4 are not conserved in other voltage-gated calcium channels
In addition, the researchers also found that the α2δ-1 subunit of Cav2.
The above findings are focused on the extracellular structure of Cav2.
▲The conformation of VSD II is different from the other three VSDs (picture source: reference [1])
The authors of this paper also found that similar to the previous Cav1.
Subsequent analysis found that the formation of this conformation is inseparable from the combination of several polar residues with the transmembrane segment S6II of VSD II
In summary, this study provides the high-definition cryo-EM structure of human Cav2.
Reference materials:
[1] Gao, S.
