Open Access
Biomedicines, volume 9, issue 11, pages 1649
Structural and Computational Study of the GroEL–Prion Protein Complex
Mamchur Aleksandra A
1
,
Moiseenko Andrei V
1
,
Panina Irina S
2
,
Yaroshevich Igor A
1
,
Kudryavtseva Sofia S
1, 3
,
Pichkur Evgeny B
4, 5
,
Sokolova Olga S.
1
,
Muronetz Vladimir I.
3, 6
,
5
Publication type: Journal Article
Publication date: 2021-11-09
PubMed ID:
34829878
General Biochemistry, Genetics and Molecular Biology
Medicine (miscellaneous)
Abstract
The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc form. Here, the molecular basis of the interactions in the GroEL–PrP complex is studied with cryo-EM and molecular dynamics approaches. The obtained cryo-EM structure shows PrP to be bound to several subunits of GroEL at the level of their apical domains. According to MD simulations, the disordered N-domain of PrP forms much more intermolecular contacts with GroEL. Upon binding to the GroEL, the N-domain of PrP begins to form short helices, while the C-domain of PrP exhibits a tendency to unfold its α2-helix. In the absence of the nucleotides in the system, these processes are manifested at the hundred nanoseconds to microsecond timescale.
Citations by journals
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1
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International Journal of Molecular Sciences
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International Journal of Molecular Sciences
1 publication, 16.67%
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Biomedicines
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Biomedicines
1 publication, 16.67%
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Microscopy and Microanalysis
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1 publication, 16.67%
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Microbiology Research
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1 publication, 16.67%
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Proceedings of the National Academy of Sciences of the United States of America
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Proceedings of the National Academy of Sciences of the United States of America
1 publication, 16.67%
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1
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Citations by publishers
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1
2
3
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
3 publications, 50%
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Oxford University Press
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Oxford University Press
1 publication, 16.67%
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Proceedings of the National Academy of Sciences (PNAS)
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Proceedings of the National Academy of Sciences (PNAS)
1 publication, 16.67%
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1
2
3
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- We do not take into account publications that without a DOI.
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- Statistics recalculated weekly.
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Mamchur A. A. et al. Structural and Computational Study of the GroEL–Prion Protein Complex // Biomedicines. 2021. Vol. 9. No. 11. p. 1649.
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Mamchur A. A., Moiseenko A. V., Panina I. S., Yaroshevich I. A., Kudryavtseva S. S., Pichkur E. B., Sokolova O. S., Muronetz V. I., Stanishneva Konovalova T. Structural and Computational Study of the GroEL–Prion Protein Complex // Biomedicines. 2021. Vol. 9. No. 11. p. 1649.
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TY - JOUR
DO - 10.3390/biomedicines9111649
UR - https://doi.org/10.3390%2Fbiomedicines9111649
TI - Structural and Computational Study of the GroEL–Prion Protein Complex
T2 - Biomedicines
AU - Mamchur, Aleksandra A
AU - Moiseenko, Andrei V
AU - Panina, Irina S
AU - Yaroshevich, Igor A
AU - Kudryavtseva, Sofia S
AU - Muronetz, Vladimir I.
AU - Pichkur, Evgeny B
AU - Sokolova, Olga S.
AU - Stanishneva Konovalova, Tatiana
PY - 2021
DA - 2021/11/09 00:00:00
PB - Multidisciplinary Digital Publishing Institute (MDPI)
SP - 1649
IS - 11
VL - 9
PMID - 34829878
SN - 2227-9059
ER -
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@article{2021_Mamchur,
author = {Aleksandra A Mamchur and Andrei V Moiseenko and Irina S Panina and Igor A Yaroshevich and Sofia S Kudryavtseva and Vladimir I. Muronetz and Evgeny B Pichkur and Olga S. Sokolova and Tatiana Stanishneva Konovalova},
title = {Structural and Computational Study of the GroEL–Prion Protein Complex},
journal = {Biomedicines},
year = {2021},
volume = {9},
publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},
month = {nov},
url = {https://doi.org/10.3390%2Fbiomedicines9111649},
number = {11},
pages = {1649},
doi = {10.3390/biomedicines9111649}
}
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Mamchur, Aleksandra A., et al. “Structural and Computational Study of the GroEL–Prion Protein Complex.” Biomedicines, vol. 9, no. 11, Nov. 2021, p. 1649. https://doi.org/10.3390%2Fbiomedicines9111649.