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LARP7.a member of the La-related proteins(LARPs),shares a conserved La module comprising the La-motif(LAM)and the RNA-recognition motif(RRM1),binding exclusively to the non-coding RNA 7SK.LARP7 is a component of the small nuclear ribonucleoprotefn(7SKsnRNP)required for the stability and function of the RNA,and implicated in the transcription termination and regulation of translation.In the current work,molecular dynamics simulations were employed to investigate the recently determined crystal structures of the La module of LARP7 in complexs with a stretch of uridines at the 3'-end of 7SK in the presence and absence of RNA and two different mutants.The structural stabilities of the four systems provided by the simulations are consistent with the experimental data.Principal component analysis(PCA)and free energy landscape(FEL)were used to explore the dominant motions and the functional dynamics between the two ends of the superhelical structures in both RNA-bound and RNA-free systems.The final values of the intramolecular angle formed by the Cα atoms of Arg30,Lys53 and Prol89 are~96° and 125° for the RNA-bound and RNA-free systems,highlighting the importance of the binding of the 3'-end of RNA 7SK for system stability.The dynamic cross-correlation maps(DCCM)were utilized to evaluate the conformational changes in different mutants,and small values were found around the residues 29-50 and 100-120 in the F168A system,whereas large values were found around the residues 120-160 and 170-189 in the E130A system.The time evolutions of the hydrogen-bond distances of the terminal uridine U-1 and Asp54 and that of the penultimate residue U-2 and Gln41 were monitored to compare their conformational changes,and the results suggest that the E130A mutant may have an important effect on the RNA binding,which is consistent with site-directed mutagenesis.This study provides some new insights into the understanding of the recognition mechanism between the La module of LARP7 and RNA 7SK.