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Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody

机译:结合POM1抗体Fab片段的病毒蛋白的结晶和初步X射线衍射分析

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摘要

Prion diseases are neurodegenerative diseases that are characterized by the conversion of the cellular prion protein PrP(c) to the pathogenic isoform PrP(sc). Several antibodies are known to interact with the cellular prion protein and to inhibit this transition. An antibody Fab fragment, Fab POM1, was produced that recognizes a structural motif of the C-terminal domain of mouse prion protein. To study the mechanism by which Fab POM1 recognizes and binds the prion molecule, the complex between Fab POM1 and the C-terminal domain of mouse prion (residues 120-232) was prepared and crystallized. Crystals of this binary complex belonged to the monoclinic space group C2, with unit-cell parameters a = 83.68, b = 106.9, c = 76.25 Å, β = 95.6°.
机译:on病毒疾病是神经退行性疾病,其特征在于细胞病毒蛋白PrP(c)转化为致病同工型PrP(sc)。已知几种抗体可与细胞病毒蛋白相互作用并抑制这种转变。产生了识别小鼠病毒蛋白C末端结构域结构基序的抗体Fab片段Fab POM1。为了研究Fab POM1识别并结合the病毒分子的机制,制备了Fab POM1和小鼠病毒C末端结构域(残基120-232)之间的复合物并进行了结晶。该二元复合物的晶体属于单斜空间群C2,其晶胞参数a = 83.68,b = 106.9,c = 76.25Å,β= 95.6°。

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