The Study Of HIL-21 And The Mechansim Of Common Subunit Intracellular Domain Receptor By Molecular Dynamics Simulations

In This work,we use molecular dynamic simulations to study the human interleukin-21(hIL-21),and research the mechanism of common subunit intracellular domain receptor.hIL-21 regulating the function and differentiation of multiple immune cells is indispensible for effective antibody response as well as anti-HIV,anti-infection,and anti-tumor response.However,due to the relatively high cost limits its wide application in clinical.In this work,we use molecular dynamic simulation to research the relationship between structure and activity,function of hIL-21 to find a more promising drugs in future.Firstly,carrying out a number of point mutations for hIL-21,using a variety of molecular dynamics analysis tools to verify the stability of the mutants,and find the more stable and active mutants.Secondly,we have an agonistic antibody when binded with the cytokine hIL-21,the activity of hIL-21 can be enhanced significantly.But the agonistic mechanism is still unknown.In this work,Basing on the experimental data,the binary complex hIL-21/2P2 which closes to real structure was obtained by using molecular docking.Its rationality was verified by molecular dynamics simulation.This binary complex can be used to research the mechanism of agonistic antibody 2P2 and cytokine hIL-21.Finaly,the common subunit intracellular domain receptor has an important role for signal transduction of hIL-21.Using molecular dynamics simulation to study the mechanism of common subunit intracellular domain receptor and biofilm DPPC,which will be prepared for further study the signal transduction mechanism of hIL-21 and its receptors.