Structural and Computational Study of the GroEL–Prion Protein Complex

The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP<sup>C</sup>, could lead to pathogenic transformation of the latter to the aggregation-prone PrP<sup>Sc</sup> form. H...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Aleksandra A. Mamchur, Andrei V. Moiseenko, Irina S. Panina, Igor A. Yaroshevich, Sofia S. Kudryavtseva, Evgeny B. Pichkur, Olga S. Sokolova, Vladimir I. Muronetz, Tatiana B. Stanishneva-Konovalova
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	molecular chaperones GroEL prion protein Cryo-EM molecular dynamics Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/512228c76fd84cecb55b734f86e49b80
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:512228c76fd84cecb55b734f86e49b80
record_format	dspace
spelling	oai:doaj.org-article:512228c76fd84cecb55b734f86e49b802021-11-25T16:50:09ZStructural and Computational Study of the GroEL–Prion Protein Complex10.3390/biomedicines91116492227-9059https://doaj.org/article/512228c76fd84cecb55b734f86e49b802021-11-01T00:00:00Zhttps://www.mdpi.com/2227-9059/9/11/1649https://doaj.org/toc/2227-9059The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP<sup>C</sup>, could lead to pathogenic transformation of the latter to the aggregation-prone PrP<sup>Sc</sup> 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.Aleksandra A. MamchurAndrei V. MoiseenkoIrina S. PaninaIgor A. YaroshevichSofia S. KudryavtsevaEvgeny B. PichkurOlga S. SokolovaVladimir I. MuronetzTatiana B. Stanishneva-KonovalovaMDPI AGarticlemolecular chaperonesGroELprion proteinCryo-EMmolecular dynamicsBiology (General)QH301-705.5ENBiomedicines, Vol 9, Iss 1649, p 1649 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	molecular chaperones GroEL prion protein Cryo-EM molecular dynamics Biology (General) QH301-705.5
spellingShingle	molecular chaperones GroEL prion protein Cryo-EM molecular dynamics Biology (General) QH301-705.5 Aleksandra A. Mamchur Andrei V. Moiseenko Irina S. Panina Igor A. Yaroshevich Sofia S. Kudryavtseva Evgeny B. Pichkur Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova Structural and Computational Study of the GroEL–Prion Protein Complex
description	The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP<sup>C</sup>, could lead to pathogenic transformation of the latter to the aggregation-prone PrP<sup>Sc</sup> 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.
format	article
author	Aleksandra A. Mamchur Andrei V. Moiseenko Irina S. Panina Igor A. Yaroshevich Sofia S. Kudryavtseva Evgeny B. Pichkur Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova
author_facet	Aleksandra A. Mamchur Andrei V. Moiseenko Irina S. Panina Igor A. Yaroshevich Sofia S. Kudryavtseva Evgeny B. Pichkur Olga S. Sokolova Vladimir I. Muronetz Tatiana B. Stanishneva-Konovalova
author_sort	Aleksandra A. Mamchur
title	Structural and Computational Study of the GroEL–Prion Protein Complex
title_short	Structural and Computational Study of the GroEL–Prion Protein Complex
title_full	Structural and Computational Study of the GroEL–Prion Protein Complex
title_fullStr	Structural and Computational Study of the GroEL–Prion Protein Complex
title_full_unstemmed	Structural and Computational Study of the GroEL–Prion Protein Complex
title_sort	structural and computational study of the groel–prion protein complex
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/512228c76fd84cecb55b734f86e49b80
work_keys_str_mv	AT aleksandraamamchur structuralandcomputationalstudyofthegroelprionproteincomplex AT andreivmoiseenko structuralandcomputationalstudyofthegroelprionproteincomplex AT irinaspanina structuralandcomputationalstudyofthegroelprionproteincomplex AT igorayaroshevich structuralandcomputationalstudyofthegroelprionproteincomplex AT sofiaskudryavtseva structuralandcomputationalstudyofthegroelprionproteincomplex AT evgenybpichkur structuralandcomputationalstudyofthegroelprionproteincomplex AT olgassokolova structuralandcomputationalstudyofthegroelprionproteincomplex AT vladimirimuronetz structuralandcomputationalstudyofthegroelprionproteincomplex AT tatianabstanishnevakonovalova structuralandcomputationalstudyofthegroelprionproteincomplex
_version_	1718412893424189440

Structural and Computational Study of the GroEL–Prion Protein Complex

Ejemplares similares