Evaluation of Fam83h Interaction with Cytoskeleton Keratin-An In-Silico Study

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NASSERI SHERKO; Mirzaie Sako; Vahabzadeh Zakaria; KHADEM ERFAN MOHAMMAD BAGHER; NIKKHOO BAHRAM; Bahrami Rad Zhila; Zamani Negar; FATHI FARDIN

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Journal: Scientific Journal of Kurdistan University of Medical Sciences Year:2022 | Volume:27 | Issue:4 (121) Page(s): 35-45

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Title

Evaluation of Fam83h Interaction with Cytoskeleton Keratin-An In-Silico Study

Author(s)

Keywords

Fam83h Protein

Keratin-5

CSNK1A1

Molecular Dynamics Simulation

Abstract

Background and Aim: Fam83h Protein is a non-secretory protein that interacts with Casein Kinase1Alpha1(CSNK1A1) through its N-terminal. Materials and Methods: In this study, the C-terminal domains of Fam83h in human and mouse were modeled using the I-TASER software for prediction of protein structure and function. The molecular dynamics (MD) simulations were performed by GROMACS version 5. 0. 2 to investigate their temporal behavior. FEL analysis was done for each model after MD. Protein-protein docking was done by PIPER to investigate the interaction of Fam83h C-terminal with cytoskeletal keratins5 as a cellular keratin model. Results: The results showed that the human protein is more stable and compact than the mouse protein. Assessment of the interaction between the C-terminal of the mouse Fam83h and Keratin-5 proteins showed the residues Arg378, Pro391, Ser663, Glu710, Arg923 in mouse Fam83h Protein made hydrogen bonds with Leu474, Arg417, Tyr453, Glu 397, Gln 396 and Glu 390 of the chain A and B of mouse Keratin-5, respectively. Human Fam83h and keratin 5 form hydrogen bonds via residues of Thr433, His447 and Arg477 and Leu473, Gly476, Glu420 and Arg407. Conclusion: According to the previous experimental reports, Fam83h can interact with keratin cytoskeleton and has a role in cancer progression. It can be concluded that Fam83h Protein can directly interact with keratin filaments through its C-terminal. Therefore, our hypothesis based on in-silico study is: non-sense mutation in C-terminal of Fam83h Protein may lead to truncated protein and subsequently disruption of keratin cytoskeleton bundling which can be regarded as a mechanism involved in cancer progression.

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APA: Copy

NASSERI, SHERKO, Mirzaie, Sako, Vahabzadeh, Zakaria, KHADEM ERFAN, MOHAMMAD BAGHER, NIKKHOO, BAHRAM, Bahrami Rad, Zhila, Zamani, Negar, & FATHI, FARDIN. (2022). Evaluation of Fam83h Interaction with Cytoskeleton Keratin-An In-Silico Study. SCIENTIFIC JOURNAL OF KURDISTAN UNIVERSITY OF MEDICAL SCIENCES, 27(4 (121) ), 35-45. SID. https://sid.ir/paper/1084524/en

Vancouver: Copy

NASSERI SHERKO, Mirzaie Sako, Vahabzadeh Zakaria, KHADEM ERFAN MOHAMMAD BAGHER, NIKKHOO BAHRAM, Bahrami Rad Zhila, Zamani Negar, FATHI FARDIN. Evaluation of Fam83h Interaction with Cytoskeleton Keratin-An In-Silico Study. SCIENTIFIC JOURNAL OF KURDISTAN UNIVERSITY OF MEDICAL SCIENCES[Internet]. 2022;27(4 (121) ):35-45. Available from: https://sid.ir/paper/1084524/en

IEEE: Copy

SHERKO NASSERI, Sako Mirzaie, Zakaria Vahabzadeh, MOHAMMAD BAGHER KHADEM ERFAN, BAHRAM NIKKHOO, Zhila Bahrami Rad, Negar Zamani, and FARDIN FATHI, “Evaluation of Fam83h Interaction with Cytoskeleton Keratin-An In-Silico Study,” SCIENTIFIC JOURNAL OF KURDISTAN UNIVERSITY OF MEDICAL SCIENCES, vol. 27, no. 4 (121) , pp. 35–45, 2022, [Online]. Available: https://sid.ir/paper/1084524/en

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