Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom.
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.
Igarashi
Tomoko
T
Department of Cardiac Physiology, National Cardiovascular Center Research Institute, 5-7-1 Fujishiro-dai, Suita, Osaka 565-8565, Japan.
Oishi
Yuko
Y
Araki
Satohiko
S
Mori
Hidezo
H
Takeda
Soichi
S
D000818:Animals; D017209:Apoptosis; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003435:Crotalid Venoms / Q000737:chemistry* / Q000302:isolation & purification; D017839:Crotalus; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D006470:Hemorrhage; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012680:Sensitivity and Specificity
D051017:Apoptosis Regulatory Proteins; D003435:Crotalid Venoms; D008666:Metalloendopeptidases; C512262:VAP2 protein, Crotalus atrox; C417254:vascular apoptosis-inducing protein 1, Crotalus atrox