通过酪氨酸硝化探究朊病毒蛋白异构体的结构差异。
Probing structural differences in prion protein isoforms by tyrosine nitration.
作者信息
Lennon Christopher W, Cox Holly D, Hennelly Scott P, Chelmo Sam J, McGuirl Michele A
机构信息
Division of Biological Sciences and the Biomolecular Structure and Dynamics Program, The University of Montana, Missoula, Montana 59812, USA.
出版信息
Biochemistry. 2007 Apr 24;46(16):4850-60. doi: 10.1021/bi0617254. Epub 2007 Mar 31.
Abstract
Two conformational isomers of recombinant hamster prion protein (residues 90-232) have been probed by reaction with two tyrosine nitration reagents, peroxynitrite and tetranitromethane. Two conserved tyrosine residues (tyrosines 149 and 150) are not labeled by either reagent in the normal cellular form of the prion protein. These residues become reactive after the protein has been converted to the beta-oligomeric isoform, which is used as a model of the fibrillar form that causes disease. After conversion, a decrease in reactivity is noted for two other conserved residues, tyrosine 225 and tyrosine 226, whereas little to no effect was observed for other tyrosines. Thus, tyrosine nitration has identified two specific regions of the normal prion protein isoform that undergo a change in chemical environment upon conversion to a structure that is enriched in beta-sheet.
摘要
已通过与两种酪氨酸硝化试剂（过氧亚硝酸盐和四硝基甲烷）反应，对重组仓鼠朊病毒蛋白（第90 - 232位氨基酸残基）的两种构象异构体进行了研究。在朊病毒蛋白的正常细胞形式中，两个保守的酪氨酸残基（酪氨酸149和酪氨酸150）均未被任何一种试剂标记。在该蛋白转变为β - 寡聚异构体后，这些残基变得具有反应活性，β - 寡聚异构体被用作导致疾病的纤维状形式的模型。转变后，另外两个保守残基酪氨酸225和酪氨酸226的反应活性降低，而其他酪氨酸几乎没有影响或没有影响。因此，酪氨酸硝化鉴定出了正常朊病毒蛋白异构体的两个特定区域，在转变为富含β - 折叠的结构时，这两个区域的化学环境会发生变化。
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