Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom
Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom
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DOI：
10.1107/s1744309106022548
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发表时间：
2006-07-01
影响因子：
0.9
通讯作者：
Takeda, Soichi
中科院分区：
文献类型：
--
作者：
Igarashi, Tomoko;Oishi, Yuko;Takeda, Soichi
VAP是出血性蛇毒毒素，属于锌金属蛋白酶的replysin家族。在体外，VAP特异性地诱导培养的血管内皮细胞凋亡。VAP具有与哺乳动物亚当斯（去整合素和金属蛋白酶）具有结构同源性的模块化结构。VAP 1是一种同源二聚体，分子量为110 kDa，其中单体通过单个二硫键连接。VAP 2与VAP 1同源，并且作为MW为55 kDa的单体存在。在目前的研究中，VAP 1和VAP 2的几种晶体形式，获得使用气相扩散法和衍射数据集收集使用SPring-8光束线。VAP 1和VAP 2的最佳晶体分别产生2.5和2.15埃分辨率的数据集。
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 metalloprotein-ases). 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 angstrom resolution, respectively.