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Structure-activity relationships of ω-Agatoxin IVA in lipid membranes.
Ryu, Jae Ha; Jung, Hoi Jong; Konishi, Shiro; Kim, Ha Hyung; Park, Zee-Yong; Kim, Jae Il.
Afiliación
  • Ryu JH; School of Life Sciences, Gwangju Institute of Science and Technology, 123, Cheomdangwagi-ro, Buk-gu, Gwangju, Republic of Korea.
  • Jung HJ; School of Life Sciences, Gwangju Institute of Science and Technology, 123, Cheomdangwagi-ro, Buk-gu, Gwangju, Republic of Korea.
  • Konishi S; Department of Neurophysiology, Kagawa School of Pharmaceutical Sciences and Institute of Neuroscience, Tokushima Bunri University, 1314-1 Shido, Sanuki-shi, Kagawa, 769-2193, Japan.
  • Kim HH; College of Pharmacy, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, Republic of Korea.
  • Park ZY; School of Life Sciences, Gwangju Institute of Science and Technology, 123, Cheomdangwagi-ro, Buk-gu, Gwangju, Republic of Korea. Electronic address: zeeyong@gist.ac.kr.
  • Kim JI; School of Life Sciences, Gwangju Institute of Science and Technology, 123, Cheomdangwagi-ro, Buk-gu, Gwangju, Republic of Korea. Electronic address: jikim@gist.ac.kr.
Biochem Biophys Res Commun ; 482(1): 170-175, 2017 Jan 01.
Article en En | MEDLINE | ID: mdl-27838299
ABSTRACT
To analyze structural features of ω-Aga IVA, a gating modifier toxin from spider venom, we here investigated the NMR solution structure of ω-Aga IVA within DPC micelles. Under those conditions, the Cys-rich central region of ω-Aga IVA still retains the inhibitor Cys knot motif with three short antiparallel ß-strands seen in water. However, 15N HSQC spectra of ω-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 ω-Aga IVA appears to assume a ß-turn like conformation within micelles, though it is disordered in water. Whole-cell patch clamp studies with several ω-Aga IVA analogs indicate that both the hydrophobic C-terminal tail and an Arg patch in the core region of ω-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.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Células de Purkinje / Membrana Celular / Canales de Calcio Tipo N / Omega-Agatoxina IVA / Membrana Dobles de Lípidos Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 2017 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Células de Purkinje / Membrana Celular / Canales de Calcio Tipo N / Omega-Agatoxina IVA / Membrana Dobles de Lípidos Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 2017 Tipo del documento: Article