Work

Tethered peptide neurotoxins display two blocking mechanisms in the K + channel pore as do their untethered analogs

Year: 2020

Type: article

Abstract: ions traversing the KcsA pore from the cytoplasm conferring voltage dependence on the toxin off rate, a classic mechanism that we observe as well with HmK in solution and for Kv1.3 channels. In contrast, two related SAK1 toxins, Hui1 and ShK, block KcsA and Kv1.3, respectively, via an arginine rather than the canonical lysine, when tethered and as free peptides.

Source: Science Advances

DOI: 10.1126/sciadv.aaz3439

Authors: Ruiming Zhao, Hui Dai, Netanel Mendelman, Jordan H. Chill, Steve A. N. Goldstein

Institutions: University of California, Irvine, Bar-Ilan University

Language: English

Topic: Ion channel regulation and function

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $4,500

Funders: United States-Israel Binational Science Foundation, National Institute of General Medical Sciences