Crystallization and preliminary X-ray diffraction analyses of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Nobuhiro SuzukiHiroshi Mizuno

Abstract

Cyclic nucleotide-gated (CNG) ion channels play pivotal roles in sensory transduction of retinal and olfactory neurons. The elapid snake toxins pseudechetoxin (PsTx) and pseudecin (Pdc) are the only known protein blockers of CNG channels. These toxins are structurally classified as cysteine-rich secretory proteins and exhibit structural features that are quite distinct from those of other known small peptidic channel blockers. This article describes the crystallization and preliminary X-ray diffraction analyses of these toxins. Crystals of PsTx belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 60.30, b = 61.59, c = 251.69 A, and diffraction data were collected to 2.25 A resolution. Crystals of Pdc also belonged to space group P2(1)2(1)2(1), with similar unit-cell parameters a = 60.71, b = 61.67, c = 251.22 A, and diffraction data were collected to 1.90 A resolution.

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Citations

Dec 8, 2009·The Journal of Biological Chemistry·Srikant RangarajuK George Chandy
Dec 25, 2008·Journal of Biochemistry·Yukiko MatsunagaTakashi Morita
Aug 2, 2018·Journal of Molecular Evolution·Kate BaumannBryan Fry

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