کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7560025 | 1491436 | 2018 | 27 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregation
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کلمات کلیدی
BSECreutzfeldt Jakob diseasePICUPQUICPrPscPrPcCJDPrPPMCAHSQCCWDSolution NMR - NMR راه حلChronic wasting disease - بیماری مزمن مزمنNMR - تشدید مغناطیسی هستهای Protein misfolding cyclic amplification - تقویت سیکل ناپایدار پروتئینBovine spongiform encephalopathy - جنون گاویcircular dichroism - رنگ تابی دورانیNuclear magnetic resonance spectroscopy - طیف سنجی رزونانس مغناطیسی هسته ایProtein misfolding - غلظت پروتئینPrion protein - پروتئین پریونrecombinant prion protein - پروتئین پریون نوترکیبcellular prion protein - پروتون پریون سلولیheteronuclear single quantum coherence - یکپارچگی کوانتومی تک هسته ای
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Prion (PrP) diseases are neurodegenerative diseases characterized by the formation of β-sheet rich, insoluble and protease resistant protein deposits (called PrPSc) that occur throughout the brain. Formation of synthetic or in vitro PrPSc can occur through on-pathway toxic oligomers. Similarly, toxic and infectious oligomers identified in cell and animal models of prion disease indicate that soluble oligomers are likely intermediates in the formation of insoluble PrPSc. Despite the critical role of prion oligomers in disease progression, little is known about their structure. In order, to obtain structural insight into prion oligomers, we generated oligomers by shaking-induced conversion of recombinant, monomeric prion protein PrPc (spanning residues 90-231). We then obtained two-dimensional solution NMR spectra of the PrPc monomer, a 40% converted oligomer, and a 94% converted oligomer. Heteronuclear single-quantum correlation (1H-15N) studies revealed that, in comparison to monomeric PrPc, the oligomer has intense amide peak signals in the N-terminal (residues 90-114) and C-terminal regions (residues 226-231). Furthermore, a core region with decreased mobility is revealed from residues ~127 to 225. Within this core oligomer region with decreased mobility, there is a pocket of increased amide peak signal corresponding to the middle of α-helix 2 and the loop between α-helices 2 and 3 in the PrPc monomer structure. Using high-resolution solution-state NMR, this work reveals detailed and divergent residue-specific changes in soluble oligomeric models of PrP.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1866, Issue 9, September 2018, Pages 982-988
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1866, Issue 9, September 2018, Pages 982-988
نویسندگان
John Paul Glaves, Carol L. Ladner-Keay, Trent C. Bjorndahl, David S. Wishart, Brian D. Sykes,