7BWI
Solution structure of recombinant APETx1
Summary for 7BWI
| Entry DOI | 10.2210/pdb7bwi/pdb |
| NMR Information | BMRB: 36345 |
| Descriptor | Kappa-actitoxin-Ael2a (1 entity in total) |
| Functional Keywords | toxin |
| Biological source | Anthopleura elegantissima (Green aggregating anemone) |
| Total number of polymer chains | 1 |
| Total formula weight | 4561.23 |
| Authors | Matsumura, K.,Kobayashi, N.,Kurita, J.,Nishimura, Y.,Yokogawa, M.,Imai, S.,Shimada, I.,Osawa, M. (deposition date: 2020-04-14, release date: 2020-12-23, Last modification date: 2024-10-16) |
| Primary citation | Matsumura, K.,Shimomura, T.,Kubo, Y.,Oka, T.,Kobayashi, N.,Imai, S.,Yanase, N.,Akimoto, M.,Fukuda, M.,Yokogawa, M.,Ikeda, K.,Kurita, J.I.,Nishimura, Y.,Shimada, I.,Osawa, M. Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization. Bmc Mol Cell Biol, 22:3-3, 2021 Cited by PubMed Abstract: Human ether-à-go-go-related gene potassium channel 1 (hERG) is a voltage-gated potassium channel, the voltage-sensing domain (VSD) of which is targeted by a gating-modifier toxin, APETx1. APETx1 is a 42-residue peptide toxin of sea anemone Anthopleura elegantissima and inhibits hERG by stabilizing the resting state. A previous study that conducted cysteine-scanning analysis of hERG identified two residues in the S3-S4 region of the VSD that play important roles in hERG inhibition by APETx1. However, mutational analysis of APETx1 could not be conducted as only natural resources have been available until now. Therefore, it remains unclear where and how APETx1 interacts with the VSD in the resting state. PubMed: 33413079DOI: 10.1186/s12860-020-00337-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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