ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
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.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 5 citations in OpenAlex.
- Scratching the Surface of an Itch: Molecular Evolution of Aculeata Venom Allergens.Journal of molecular evolution · 2018Article
- Potassium channel modulation by a toxin domain in matrix metalloprotease 23.The Journal of biological chemistry · 2010Article
- Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain.Acta crystallographica. Section D, Biological crystallography · 2008Article
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5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
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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