Structure-activity relationships of omega-Agatoxin IVA in lipid membranes
- Authors
- Ryu, Jae Ha; Jung, Hoi Jong; Konishi, Shiro; Kim, Ha Hyung; Park, Zee-Yong; Kim, Jae Il
- Issue Date
- Jan-2017
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- omega-Agatoxin IVA; Gating modifier toxin; Cav2.1
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.482, no.1, pp 170 - 175
- Pages
- 6
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 482
- Number
- 1
- Start Page
- 170
- End Page
- 175
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/4920
- DOI
- 10.1016/j.bbrc.2016.11.025
- ISSN
- 0006-291X
1090-2104
- Abstract
- To analyze structural features of omega-Aga IVA, a gating modifier toxin from spider venom, we here investigated the NMR solution structure of omega-Aga IVA within DPC micelles. Under those conditions, the Cys-rich central region of omega-Aga IVA still retains the inhibitor Cys knot motif with three short antiparallel beta-strands seen in water. However, N-15 HSQC spectra of omega-Aga IVA within micelles revealed that there are radical changes to the toxin's C-terminal tail and several loops upon binding to micelles. The C-terminal tail of omega-Aga IVA appears to assume a beta-turn like conformation within micelles, though it is disordered in water. Whole-cell patch clamp studies with several omega-Aga IVA analogs indicate that both the hydrophobic C-terminal tail and an Arg patch in the core region of omega-Aga IVA are critical for Cav2.1 blockade. These results suggest that the membrane environment stabilizes the structure of the toxin, enabling it to act in a manner similar to other gating modifier toxins, though its mode of interaction with the membrane and the channel is unique. (C) 2016 Elsevier Inc. All rights reserved.
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