Referenced in: none

Automatically associated channels: Kv1.3 , Slo1

Title: Structural and functional analysis of natrin, a venom protein that targets various ion channels.

Authors: Feng Wang, He Li, Ming-na Liu, Hui Song, Hong-mei Han, Qiong-Ling Wang, Chang-chen Yin, Yuan-cong Zhou, Zhi Qi, Yu-yan Shu, Zheng-jiong Lin, Tao Jiang

Journal, date & volume: Biochem. Biophys. Res. Commun., 2006 Dec 15 , 351, 443-8

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/17070778

Abstract
Cysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our study, crystals of natrin were obtained in two different crystal forms and the structure of one of them was solved at a resolution of 1.68A. Our electrophysiological experiments indicated that natrin can block the ion channel currents of the voltage-gated potassium channel Kv1.3. Docking analyses of the interaction between natrin and Kv1.3 revealed a novel interaction pattern different from the two previously reported K(+) channel inhibition models termed "functional dyad" and "basic ring". These findings offered new insights into the function of natrin and how the specific interactions between CRISPs and different ion channels can be achieved.