2GIZ

Structural and functional analysis of Natrin, a member of crisp-3 family blocks a variety of ion channels

Summary for 2GIZ

• Entry DOI: 10.2210/pdb2giz/pdb
• Descriptor: Natrin-1 (2 entities in total)
• Functional Keywords: crisp, blocker, electrophysiology, docking, toxin
• Biological source: Naja atra (Chinese cobra)
• Cellular location: Secreted: Q7T1K6
• Total number of polymer chains: 2
• Total formula weight: 49962.18

Authors

Jiang, T.,Wang, F.,Li, H.,Yin, C.,Zhou, Y.,Shu, Y.,Qi, Z.,Lin, Z. (deposition date: 2006-03-30, release date: 2006-11-28, Last modification date: 2024-10-30)

Primary citation

Wang, F.,Li, H.,Liu, M.,Song, H.,Han, H.,Wang, Q.,Yin, C.,Zhou, Y.,Qi, Z.,Shu, Y.,Lin, Z.,Jiang, T.
Structural and functional analysis of natrin, a venom protein that targets various ion channels
Biochem.Biophys.Res.Commun., 351:443-448, 2006

PubMed 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.

PubMed: 17070778
DOI: 10.1016/j.bbrc.2006.10.067

Experimental method

X-RAY DIFFRACTION (1.68 Å)