Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants

Zhang, Jiapu

doi:10.1016/j.jtbi.2010.01.024

Cited by 34 publications

(32 citation statements)

References 34 publications

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“…10,41,43,45,46,49,50,52,63,65 The measurements of flexibility has been carried out mainly using RMSF. 43,45,46,49,52,63 Here, we use the angular dispersion index (ADI) of the helices-ADI_α 2 and ADI_α 3 -for characterizing their flexibility: the larger the ADI_α 2 and ADI_α 3 are, the larger are the flexibility and/or the local rearrangements (see Materials and Methods for details).…”

Section: Resultsmentioning

confidence: 99%

Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases

Rossetti

Cong

Caliandro

et al. 2011

Journal of Molecular Biology

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Section: Resultsmentioning

confidence: 99%

Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases

Rossetti

Cong

Caliandro

et al. 2011

Journal of Molecular Biology

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“…Moreover, the wild-type RaPrPC protein shows a much higher structural stability compared with its S173N and I214V mutants, which was confirmed by molecular dynamics simulation [50]. Significantly, RaPrP C possesses a unique electrostatic charge distribution, [37,38,40,104].…”

Section: Prpmentioning

confidence: 67%

Prion protein oligomer and its neurotoxicity

Huang

Lian

Wen

et al. 2013

ABBS

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The prion diseases, also known as transmissible spongiform encephalopathies, are fatal neurodegenerative disorders. According to the 'protein only' hypothesis, the key molecular event in the pathogenesis of prion disease is the conformational conversion of the host-derived cellular prion protein (PrP C ) into a misfolded form (scrapie PrP, PrP Sc ). Increasing evidence has shown that the most infectious factor is the smaller subfibrillar oligomers formed by prion proteins. Both the prion oligomer and PrP Sc are rich in b-sheet structure and resistant to the proteolysis of proteinase K. The prion oligomer is soluble in physiologic environments whereas PrP Sc is insoluble. Various prion oligomers are formed in different conditions. Prion oligomers exhibited more neurotoxicity both in vitro and in vivo than the fibrillar forms of PrP Sc , implying that prion oligomers could be potential drug targets for attacking prion diseases. In this article, we describe recent experimental evidence regarding prion oligomers, with a special focus on prion oligomer formation and its neurotoxicity.

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“…The MD methods employed are the same as the previous studies (Zhang & Zhang, 2013Zhang, 2010Zhang, & 2011c. Briefly, all simulations used the ff03 force field of the AMBER 11 package (Case et al, 2010).…”

Section: Methodsmentioning

confidence: 99%

A review on the salt bridge ASP177-ARG163 (O–N) of wild-type rabbit prion protein

Zhang

Wang

2016

Journal of Biomolecular Structure and Dynamics

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Abstract:Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer, elks, humans and mice etc., but rabbits have a low susceptibility to be infected by prion diseases with respect to other species. The stability of rabbit prion protein is due to its highly ordered β2-α2 loop (PLoS One 5(10) e13273 X-ray file of the rabbit prion protein, we can clearly observe this salt bridge. This article analyses the NMR and X-ray structures and gives an answer to the above question: the salt bridge presents at pH 6.5 in the X-ray structure is simply gone at pH 4.5 in the NMR structure is simply due to the different pH values that impact electrostatics at the salt bridge and hence also impact the structures. Moreover, some molecular dynamics simulation results of the X-ray structure are reported in this article to reveal the secrets of the structural stability of rabbit prion protein.

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Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants

Cited by 34 publications

References 34 publications

Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases

Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases

Prion protein oligomer and its neurotoxicity

A review on the salt bridge ASP177-ARG163 (O–N) of wild-type rabbit prion protein

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