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Title
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Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom.
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Authors
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T.Igarashi,
Y.Oishi,
S.Araki,
H.Mori,
S.Takeda.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2006,
62,
688-691.
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PubMed id
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Abstract
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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 angstroms resolution, respectively.
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