Document Type : Research Paper

Authors

• s.shahrbanoo jafari ¹
• Rahman Emamzadeh ¹
• Mahboobeh Nazari ^{2, 3}
• Sepideh Jafari ⁴
• Mohamad Reza Ganjalikhany ¹

¹ Department of Cell and Molecular Biology & Microbiology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, I.R. of Iran

² Endocrine Research Center, Institute of Endocrinology and Metabolism, Iran University of Medical Sciences, Tehran, I.R. of Iran

³ Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, I.R. of Iran

⁴ Department of Cell and Molecular Biology & Microbiology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, I.R. of Iran

Abstract

FSTL1 (follistatin-like 1) is a secretory extracellular glycoprotein that is a member of the SPARC-Fst family of proteins, a group that has an FK domain and an EF-hand domain pair. FSTL1 is involved in regulating survival, proliferation, differentiation, cell migration, organ development, as well as carcinogenesis, and metastasis. Despite extensive studies on FSTL1, little structural information on this important biomolecule is available. Predicting the structural and dynamic movements of the FSTL1 protein can be useful and effective in gaining a better understanding of most of the biological processes in which this important molecule is involved. Therefore, in the present study, molecular dynamics simulation was used to evaluate the flexibility of the FK domain of FSTL1 protein, which is essential for the function of this protein. The simulation results indicate that the disulfide-free protein has a higher RMSD than the natural protein. The RMSF diagram showed a significant increase in structural changes in the disulfide-free protein in the range of residues 9-18, 31, 62-52, 72, and 160-147. Also, in protein without sulfide bond, 36-52, the radius of gyration was significantly increased at 1 to 3 nanoseconds after the start of the simulation. These findings indicate that deletion of the 36-32 disulfide bond in the FK domain of the FSTL1 protein increases the flexibility of the protein. These findings also suggest that this bond could be a potential target region for targeted mutagenicity studies to increase of flexibility of molecules.

Keywords

• FSTL1
• Disulfide bond
• Molecular dynamics simulation
• Flexibility

Main Subjects

• Bioinformatics