Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers

Sabareesan A. T.; Udgaonkar Jayant B.

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Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers

机译：on病毒蛋白无序回文区域内的致病突变诱导其中的结构并加速错误折叠的寡聚体的形成

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Little is understood about how the intrinsically disordered N-terminal region (NTR) of the prion protein modulates its misfolding and aggregation, which lead to prion disease. In this study, two pathogenic mutations, G113V and A116V, in the palindromic region of the NTR are shown to have no effect on the structure, stability, or dynamics of native mouse prion protein (moPrP) but nevertheless accelerate misfolding and oligomerization. For wild-type moPrP, misfolding and oligomerization appear to occur concurrently, while for both mutant variants, oligomerization is shown to precede misfolding. Kinetic hydrogen deuterium exchange-mass spectrometry experiments show that sequence segment 89-132 from the NTR becomes structured, albeit weakly, during the oligomerization of both mutant variants. Importantly, this structure formation occurs prior to structural conversion in the C-terminal domain and appears to be the reason that the formation of misfolded oligomers is accelerated by the pathogenic mutations. (C) 2016 Elsevier Ltd. All rights reserved.

机译：对于the病毒蛋白的内在无序的N末端区域（NTR）如何调节其错误折叠和聚集（导致病毒病），人们知之甚少。在这项研究中，NTR回文区的两个致病性突变G113V和A116V对天然小鼠ion病毒蛋白（moPrP）的结构，稳定性或动力学没有影响，但是却加速了错误折叠和寡聚。对于野生型moPrP，错误折叠和寡聚似乎同时发生，而对于两个突变体变体，都显示寡聚先于错误折叠。动力学氢氘交换质谱实验表明，在两个突变体变体寡聚化过程中，来自NTR的序列段89-132都变得结构化，尽管微弱。重要的是，这种结构形成发生在C-末端结构域中的结构转化之前，并且似乎是由于病原性突变加速了错误折叠的低聚物形成的原因。（C）2016 Elsevier Ltd.保留所有权利。

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《Journal of Molecular Biology》 |2016年第20期|共13页
作者
Sabareesan A. T.; Udgaonkar Jayant B.;
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cellular prion protein; circular dichroism; hydrogen deuterium exchange-mass spectrometry; size-exclusion chromatography;

机译：细胞病毒蛋白圆二色性氢氘交换质谱法体积排阻色谱;

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1. Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers [J] . Sabareesan A. T., Udgaonkar Jayant B. Journal of Molecular Biology . 2016,第20期

机译：on病毒蛋白无序回文区域内的致病突变诱导其中的结构并加速错误折叠的寡聚体的形成
2. Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans [J] . Shaoman Yin, Nancy Pham, Shuiliang Yu, Proceedings of the National Academy of Sciences of the United States of America . 2007,第18期

机译：具有致病性突变的人类病毒蛋白具有共同的构象变化，从而增强了与糖胺聚糖的结合
3. Prion Proteins with Pathogenic and Protective Mutations Show Similar Structure and Dynamics [J] . Sung-Hun Bae Giuseppe Legname Ana Serban Stanley B. Prusiner Peter E. Wright and H. Jane Dyson Biochemistry . 2009,第34期

机译：具有致病性和保护性突变的病毒蛋白显示相似的结构和动力学
4. Studies on the Effect of Pathogenic Mutations in the Transmembrane Region Structure of FGFR3 [C] . Hiroko Tamagaki, Yusuke Furukawa, Chihiro Matsushita Japanese peptide symposium . 2010

机译：致病性突变在FGFR3跨膜区结构中致病性突变的影响研究
5. Theoretical Model for the Conformation of the Misfolded Prion Protein. [D] . Orr, Jamie Francesca. 2011

机译：错误折叠的Pri病毒蛋白构象的理论模型。
6. Pathogenic Mutations within the Hydrophobic Domain of the Prion Protein Lead to the Formation of Protease-Sensitive Prion Species with Increased Lethality [O] . Bradley M. Coleman, Christopher F. Harrison, Belinda Guo, 2014

机译：on病毒蛋白疏水域内的致病性突变导致蛋白酶敏感性on病毒物种的致死性增加
7. Pathogenic Mutations within the Hydrophobic Domain of the Prion Protein Lead to the Formation of Protease-Sensitive Prion Species with Increased Lethality [O] . orcid:0000-0003-2146-8561, orcid:0000-0002-7362-7176, orcid:0000-0001-5581-2354, 2014

机译：朊蛋白疏水结构域内的致病突变导致蛋白酶敏感的朊病毒种类的形成具有增加的致死率

Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers

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