Modeling of streptokinase mutants and evaluation of their Intermolecular interaction with microplasmin

Modeling of streptokinase mutants and evaluation of their Intermolecular interaction with microplasmin
Narges Norouzzadeh Alinodehi,^1,* Reza Arabi Mianroodi,²
1. Department of Genetics and Biotechnology, School of Biological Science, Varamin-Pishva Branch, Islamic Azad University, Varamin, Iran.
2. R&D Department, Research and Production Complex, Pasteur Institute of Iran, Karaj, Iran
Introduction: Thrombosis of blood vessels in different organs especially in heart can lead to irreversible consequences if not acted in time. Streptokinase as one of the most important thrombolytic drugs may be engineered to be used repeatedly and safely for patients who suffer from such a dangerous disease.
Methods: Mutant streptokinase proteins, having cysteine residues in their structure, were modeled and docked with their counterpart in the active enzymatic complex and their intermolecular interaction was compared to the intact streptokinase.
Results: The results showed that the mutant protein containing cysteine at 263 and 319 sites increased 6.89% of buried surface area but on the other hand RMSD between alpha carbons from the lowest energy structure increased from 1.1 to 1.3
Conclusion: These results showed that these cysteine residues may confer more flexibility to streptokinase structure and increase the ability of the activator complex for higher activity. Experimental analysis is required to be carried out to demonstrate this primary results
Keywords: Mutant, streptokinase, docking , RMSD