Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis

Ezrin (EZR) is a crucial linker between the actin cytoskeleton and the plasma membrane. It interacts with proteins involved in cancer-related signaling pathways. To assess the impact of nonsynonymous single nucleotide polymorphisms (nsSNPs) on EZR structure and function, we employed bioinformatics t...

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Main Authors: Sadia Akter, Mohtasim Fuad, Zimam Mahmud, Sonia Tamanna, Mohammad Sayem, Khalid Hasan Raj, Md. Zakir Hossain Howlader
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Biochemistry and Biophysics Reports
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Online Access:http://www.sciencedirect.com/science/article/pii/S2405580825000597
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author Sadia Akter
Mohtasim Fuad
Zimam Mahmud
Sonia Tamanna
Mohammad Sayem
Khalid Hasan Raj
Md. Zakir Hossain Howlader
author_facet Sadia Akter
Mohtasim Fuad
Zimam Mahmud
Sonia Tamanna
Mohammad Sayem
Khalid Hasan Raj
Md. Zakir Hossain Howlader
author_sort Sadia Akter
collection DOAJ
description Ezrin (EZR) is a crucial linker between the actin cytoskeleton and the plasma membrane. It interacts with proteins involved in cancer-related signaling pathways. To assess the impact of nonsynonymous single nucleotide polymorphisms (nsSNPs) on EZR structure and function, we employed bioinformatics tools (SIFT, PolyPhen-2, PROVEAN, PhD-SNP, SNPs&GO, SuSPect, and FATHMM) and identified deleterious variants. Stability analyses using MUpro, mCSM, I-Mutant 2.0, and DynaMut2 revealed six destabilizing nsSNPs (F240S, H288D, I248T, L59Q, L125S, and L225P). Structural modeling using HOPE, MutPred2, AlphaFold, Swiss-Model, and protein-protein docking using HADDOCK 2.4 assessed the impact on the EZR-EBP50 complex. Binding free energy calculations, salt bridge analysis, and interface residue mapping further confirmed that the L225P, F240S, and I248T mutations significantly impaired EZR-EBP50 interaction, potentially disrupting key signaling pathways. Molecular dynamics simulations indicated that mutant EZR proteins exhibited reduced stability, flexibility, and hydrogen bonding. This first comprehensive in silico analysis of EZR highlights pathogenic nsSNPs that may contribute to disease progression. These findings provide a foundation for experimental validation and may inform targeted therapies for EZR-related pathologies.
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spelling doaj-art-1ae4bd221ae54ceaa631b0a77d5c22d92025-08-20T02:37:38ZengElsevierBiochemistry and Biophysics Reports2405-58082025-06-014210197210.1016/j.bbrep.2025.101972Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesisSadia Akter0Mohtasim Fuad1Zimam Mahmud2Sonia Tamanna3Mohammad Sayem4Khalid Hasan Raj5Md. Zakir Hossain Howlader6Department of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshDepartment of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshCorresponding author.; Department of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshDepartment of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshDepartment of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshDepartment of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshDepartment of Biochemistry and Molecular Biology, University of Dhaka, Dhaka, 1000, BangladeshEzrin (EZR) is a crucial linker between the actin cytoskeleton and the plasma membrane. It interacts with proteins involved in cancer-related signaling pathways. To assess the impact of nonsynonymous single nucleotide polymorphisms (nsSNPs) on EZR structure and function, we employed bioinformatics tools (SIFT, PolyPhen-2, PROVEAN, PhD-SNP, SNPs&GO, SuSPect, and FATHMM) and identified deleterious variants. Stability analyses using MUpro, mCSM, I-Mutant 2.0, and DynaMut2 revealed six destabilizing nsSNPs (F240S, H288D, I248T, L59Q, L125S, and L225P). Structural modeling using HOPE, MutPred2, AlphaFold, Swiss-Model, and protein-protein docking using HADDOCK 2.4 assessed the impact on the EZR-EBP50 complex. Binding free energy calculations, salt bridge analysis, and interface residue mapping further confirmed that the L225P, F240S, and I248T mutations significantly impaired EZR-EBP50 interaction, potentially disrupting key signaling pathways. Molecular dynamics simulations indicated that mutant EZR proteins exhibited reduced stability, flexibility, and hydrogen bonding. This first comprehensive in silico analysis of EZR highlights pathogenic nsSNPs that may contribute to disease progression. These findings provide a foundation for experimental validation and may inform targeted therapies for EZR-related pathologies.http://www.sciencedirect.com/science/article/pii/S2405580825000597EZR geneNonsynonymous mutationsFERM domainERM binding protein 50Ezrin binding domainMolecular docking
spellingShingle Sadia Akter
Mohtasim Fuad
Zimam Mahmud
Sonia Tamanna
Mohammad Sayem
Khalid Hasan Raj
Md. Zakir Hossain Howlader
Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
Biochemistry and Biophysics Reports
EZR gene
Nonsynonymous mutations
FERM domain
ERM binding protein 50
Ezrin binding domain
Molecular docking
title Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
title_full Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
title_fullStr Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
title_full_unstemmed Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
title_short Comprehensive in silico characterization of nonsynonymous SNPs in the human ezrin (EZR) gene and their role in disease pathogenesis
title_sort comprehensive in silico characterization of nonsynonymous snps in the human ezrin ezr gene and their role in disease pathogenesis
topic EZR gene
Nonsynonymous mutations
FERM domain
ERM binding protein 50
Ezrin binding domain
Molecular docking
url http://www.sciencedirect.com/science/article/pii/S2405580825000597
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