Role of the disulfide bond on the structure and activity of μ-conotoxin PIIIA in the inhibition of NaV1.4-Reference-Cited by-同舟云学术

Role of the disulfide bond on the structure and activity of μ-conotoxin PIIIA in the inhibition of NaV1.4

Published:2019 Issue:2 Volume:9 Page:668-674
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Xu Xiaoxiao¹²³⁴⁵,Xu Qingliang¹²³⁴⁵,Chen Fangling¹²³⁴⁵,Shi Juan¹²³⁴⁵,Liu Yuntian¹²³⁴⁵^ORCID,Chu Yanyan⁶⁷⁸,Wan Shengbiao¹²³⁴⁵,Jiang Tao¹²³⁴⁵,Yu Rilei¹²³⁴⁵^ORCID

Affiliation:

1. Key Laboratory of Marine Drugs

2. Chinese Ministry of Education

3. School of Medicine and Pharmacy

4. Ocean University of China

5. Qingdao

6. Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology

7. Qingdao 266003

8. China

Abstract

μ-Conotoxin PIIIA, a peptide toxin isolated from Conus purpurascens, blocks the skeletal muscle voltage-gated sodium channel Na_V1.4 with significant potency.

Funder

National Natural Science Foundation of China

Qingdao National Laboratory for Marine Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/RA/C8RA06103C

Reference43 articles.

1. Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution

2. Expression of functional sodium channels from cloned cDNA