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Conformational diversity in prion protein variants influences intermolecular beta-sheet formation

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Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. / Lee, Seungjoo; Antony, Lizamma; Hartmann, Rune; Knaus, Karen J; Surewicz, Krystyna; Surewicz, Witold K; Yee, Vivien C.

I: E M B O Journal, Bind 29, Nr. 1, 2010, s. 251-62.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Lee, S, Antony, L, Hartmann, R, Knaus, KJ, Surewicz, K, Surewicz, WK & Yee, VC 2010, 'Conformational diversity in prion protein variants influences intermolecular beta-sheet formation', E M B O Journal, bind 29, nr. 1, s. 251-62. https://doi.org/10.1038/emboj.2009.333

APA

Lee, S., Antony, L., Hartmann, R., Knaus, K. J., Surewicz, K., Surewicz, W. K., & Yee, V. C. (2010). Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. E M B O Journal, 29(1), 251-62. https://doi.org/10.1038/emboj.2009.333

CBE

Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC. 2010. Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. E M B O Journal. 29(1):251-62. https://doi.org/10.1038/emboj.2009.333

MLA

Vancouver

Author

Lee, Seungjoo ; Antony, Lizamma ; Hartmann, Rune ; Knaus, Karen J ; Surewicz, Krystyna ; Surewicz, Witold K ; Yee, Vivien C. / Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. I: E M B O Journal. 2010 ; Bind 29, Nr. 1. s. 251-62.

Bibtex

@article{5f61d480ff5a11de9c17000ea68e967b,
title = "Conformational diversity in prion protein variants influences intermolecular beta-sheet formation",
abstract = "A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants: three of wild-type (WT) PrP containing V129, and four of the familial variants D178N and F198S, containing either M129 or V129. Comparison of these structures with each other and with previously published WT PrP structures containing M129 revealed that only WT PrPs were found to crystallize as domain-swapped dimers or closed monomers; the four mutant PrPs crystallized as non-swapped dimers. Three of the four mutant PrPs aligned to form intermolecular beta-sheets. Several regions of structural variability were identified, and analysis of their conformations provides an explanation for the structural features, which can influence the formation and conformation of intermolecular beta-sheets involving the M/V129 polymorphic residue.",
author = "Seungjoo Lee and Lizamma Antony and Rune Hartmann and Knaus, {Karen J} and Krystyna Surewicz and Surewicz, {Witold K} and Yee, {Vivien C}",
year = "2010",
doi = "10.1038/emboj.2009.333",
language = "English",
volume = "29",
pages = "251--62",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell Publishing Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Conformational diversity in prion protein variants influences intermolecular beta-sheet formation

AU - Lee, Seungjoo

AU - Antony, Lizamma

AU - Hartmann, Rune

AU - Knaus, Karen J

AU - Surewicz, Krystyna

AU - Surewicz, Witold K

AU - Yee, Vivien C

PY - 2010

Y1 - 2010

N2 - A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants: three of wild-type (WT) PrP containing V129, and four of the familial variants D178N and F198S, containing either M129 or V129. Comparison of these structures with each other and with previously published WT PrP structures containing M129 revealed that only WT PrPs were found to crystallize as domain-swapped dimers or closed monomers; the four mutant PrPs crystallized as non-swapped dimers. Three of the four mutant PrPs aligned to form intermolecular beta-sheets. Several regions of structural variability were identified, and analysis of their conformations provides an explanation for the structural features, which can influence the formation and conformation of intermolecular beta-sheets involving the M/V129 polymorphic residue.

AB - A conformational transition of normal cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)) is believed to be a central event in the transmission of the devastating neurological diseases known as spongiform encephalopathies. The common methionine/valine polymorphism at residue 129 in the PrP influences disease susceptibility and phenotype. We report here seven crystal structures of human PrP variants: three of wild-type (WT) PrP containing V129, and four of the familial variants D178N and F198S, containing either M129 or V129. Comparison of these structures with each other and with previously published WT PrP structures containing M129 revealed that only WT PrPs were found to crystallize as domain-swapped dimers or closed monomers; the four mutant PrPs crystallized as non-swapped dimers. Three of the four mutant PrPs aligned to form intermolecular beta-sheets. Several regions of structural variability were identified, and analysis of their conformations provides an explanation for the structural features, which can influence the formation and conformation of intermolecular beta-sheets involving the M/V129 polymorphic residue.

U2 - 10.1038/emboj.2009.333

DO - 10.1038/emboj.2009.333

M3 - Journal article

C2 - 19927125

VL - 29

SP - 251

EP - 262

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 1

ER -