Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|62|7|688-691
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.62, Iss.7, 2006-07, pp. : 688-691
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Abstract
VAPs are haemorrhagic snake‐venom toxins belonging to the reprolysin family of zinc metalloproteinases. In vitro, VAPs induce apoptosis specifically in cultured vascular endothelial cells. VAPs have a modular structure that bears structural homology to mammalian ADAMs (a disintegrin and metalloproteinases). VAP1 is a homodimer with a MW of 110 kDa in which the monomers are connected by a single disulfide bridge. VAP2 is homologous to VAP1 and exists as a monomer with a MW of 55 kDa. In the current study, several crystal forms of VAP1 and VAP2 were obtained using the vapour‐diffusion method and diffraction data sets were collected using SPring‐8 beamlines. The best crystals of VAP1 and VAP2 generated data sets to 2.5 and 2.15 Å resolution, respectively.
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