1xta

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spinqualitylabelsall models 1xta, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Natrin, a snake venom CRISP from Taiwan cobra (Naja atra)

Overview

Cysteine-rich secretory proteins (CRISPs) play an important role in the, innate immune system and are transcriptionally regulated by androgens in, several tissues. The proteins are mostly found in the epididymis and, granules of mammals, whilst a number of snake venoms also contain, CRISP-family proteins. The natrin protein from the venom of Naja atra, (Taiwan cobra), which belongs to a family of CRISPs and has a, cysteine-rich C-terminal amino-acid sequence, has been purified using a, three-stage chromatography procedure and crystals suitable for X-ray, analysis have been obtained using the hanging-drop vapour-diffusion, method. X-ray diffraction data were collected to 1.58 A resolution using, synchrotron radiation; the crystals belong to space group C222(1), with, unit-cell parameters a = 59.172, b = 65.038, c = 243.156 A. There are two, protein molecules in the asymmetric unit and the Matthews coefficient is, estimated to be 2.35 A3 Da(-1), corresponding to a solvent content of, 47.60%.

About this Structure

1XTA is a Single protein structure of sequence from Naja atra. Full crystallographic information is available from OCA.

Reference

Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom., Wang YL, Goh KX, Wu WG, Chen CJ, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1912-5. Epub 2004, Sep 23. PMID:15388950

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