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000889873 1001_ $$0P:(DE-HGF)0$$aCaruso, Icaro P.$$b0
000889873 245__ $$aBiophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
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000889873 520__ $$aThe human respiratory syncytial virus (hRSV) M2-1 protein functions as a processivity and antitermination factor of the viral polymerase complex. Here, the first evidence that the hRSV M2-1 core domain (cdM2-1) alone has an unfolding activity for long RNAs is presented and the biophysical and dynamic characterization of the cdM2-1/RNA complex is provided. The main contact region of cdM2-1 with RNA was the α1-α2-α5-α6 helix bundle, which suffered local conformational changes and promoted the RNA unfolding activity. This activity may be triggered by base-pairing recognition. RNA molecules wrap around the whole cdM2-1, protruding their termini over the domain. The α2-α3 and α3-α4 loops of cdM2-1 were marked by an increase in picosecond internal motions upon RNA binding, even though they are not directly involved in the interaction. The results revealed that the cdM2-1/RNA complex originates from a fine-tuned binding, contributing to the unraveling interaction aspects necessary for M2-1 activity.
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000889873 7001_ $$0P:(DE-HGF)0$$aGuimarães, Giovana C.$$b1
000889873 7001_ $$0P:(DE-HGF)0$$aMachado, Vitor B.$$b2
000889873 7001_ $$0P:(DE-HGF)0$$aFossey, Marcelo A.$$b3
000889873 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b4$$ufzj
000889873 7001_ $$00000-0001-6046-7006$$aAlmeida, Fabio C. L.$$b5
000889873 7001_ $$0P:(DE-HGF)0$$aSouza, Fátima P.$$b6$$eCorresponding author
000889873 773__ $$0PERI:(DE-600)1495529-5$$a10.1128/JVI.01505-20$$gVol. 94, no. 23, p. e01505-20/jvi/94/23/JVI.01505-20.atom$$n23$$p e01505-20$$tJournal of virology$$v94$$x1098-5514$$y2020
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