Next Article in Journal
A Promising Biocompatible Platform: Lipid-Based and Bio-Inspired Smart Drug Delivery Systems for Cancer Therapy
Previous Article in Journal
Genetic and Epigenetic Modifiers of Alcoholic Liver Disease
 
 
Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
Journals
IJMS
Volume 19
Issue 12
10.3390/ijms19123858
ijms-logo
Submit to this Journal Review for this Journal Propose a Special Issue
► Article Menu

Article Menu

share Share announcement Help format_quote Cite question_answer Discuss in SciProfiles
first_page
settings
Order Article Reprints
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Article

Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP

by
Milan Hodošček
1 and
Nadia Elghobashi-Meinhardt
2,*
1
National Institute of Chemistry, Hajdrihova 19, 1001 Ljubljana, Slovenia
2
Department of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(12), 3858; https://doi.org/10.3390/ijms19123858
Submission received: 23 October 2018 / Revised: 21 November 2018 / Accepted: 28 November 2018 / Published: 3 December 2018
(This article belongs to the Section Molecular Biophysics)
Browse Figures
Versions Notes

Abstract

A combination of molecular dynamics (MD) simulations and computational analyses uncovers structural features that may influence substrate passage and exposure to the active sites within the proteolytic chamber of the 20S proteasome core particle (CP). MD simulations of the CP reveal relaxation dynamics in which the CP slowly contracts over the 54 ns sampling period. MD simulations of the SyringolinA (SylA) inhibitor within the proteolytic B 1 ring chamber of the CP indicate that favorable van der Waals and electrostatic interactions account for the predominant association of the inhibitor with the walls of the proteolytic chamber. The time scale required for the inhibitor to travel from the center of the proteolytic chamber to the chamber wall is on the order of 4 ns, accompanied by an average energetic stabilization of approximately −20 kcal/mol.
Keywords: proteasome; core particle (CP); SyringolinA inhibitor; proteolytic; active site; molecular dynamics (MD); simulations; electrostatic interactions proteasome; core particle (CP); SyringolinA inhibitor; proteolytic; active site; molecular dynamics (MD); simulations; electrostatic interactions

Share and Cite

MDPI and ACS Style

Hodošček, M.; Elghobashi-Meinhardt, N. Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP. Int. J. Mol. Sci. 2018, 19, 3858. https://doi.org/10.3390/ijms19123858

AMA Style

Hodošček M, Elghobashi-Meinhardt N. Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP. International Journal of Molecular Sciences. 2018; 19(12):3858. https://doi.org/10.3390/ijms19123858

Chicago/Turabian Style

Hodošček, Milan, and Nadia Elghobashi-Meinhardt. 2018. "Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP" International Journal of Molecular Sciences 19, no. 12: 3858. https://doi.org/10.3390/ijms19123858

APA Style

Hodošček, M., & Elghobashi-Meinhardt, N. (2018). Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP. International Journal of Molecular Sciences, 19(12), 3858. https://doi.org/10.3390/ijms19123858

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop