JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2024  1,200
2023  1,500
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 59(2025) N 3 p. 449-457; DOI 10.1134/S0026893325700116 Full Text

A.A. Sargsyan1,2, N.G. Muradyan1, V.G. Arakelov1, A.K. Paronyan1,2, G.G. Arakelov1,2*, K.B. Nazaryan1,2

In silico Screening of Protein-Protein Interaction Modulators Using the p53 and 14-3-3y Proteins as an Example

1Laboratory of Computational Modeling of Biological Processes, Institute of Molecular Biology, National Academy of Sciences of the Republic of Armenia (NAS RA), Yerevan, 0014 Armenia
2Russian-Armenian University, Yerevan, 0051 Armenia


*g.g.arakelov@rau.am
Received - 2024-08-10; Revised - 2024-12-23; Accepted - 2024-12-29

The study of the p53 protein and its interactions with other proteins is key to understanding the mechanisms by which p53 affects tumorigenesis. Mutations in the TP53 gene, which occur in approximately 50% of human cancers, often disrupt its function, highlighting its key role in tumorigenesis. Although structurally challenging due to the presence of unstructured regions, p53 has a well-documented role in DNA damage signaling and cancer progression. In this study, the interaction between p53 and 14-3-3γ monomers was studied using in silico methods. Using tertiary structure modeling, molecular dynamics, molecular docking, and virtual ligand screening, we identified small molecule compounds that can modulate the interaction of p53 with 14-3-3γ. Key findings of the study include identification of a ligand binding pocket in the p53-14-3-3γ interaction interface, generation of full-length models of 14-3-3γ and p53 using in silico methods, and selection of potential protein-protein modulators with high affinity for the proteins under study.

p53, 14-3-3γ, protein-protein interaction modulators, disordered proteins, molecular dynamics, virtual screening



JMB-FOOTER RAS-JOURNALS