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000139657 1001_ $$0P:(DE-Juel1)132019$$aSchwarten, Melanie$$b0$$eCorresponding author$$ufzj
000139657 245__ $$aInteraction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites
000139657 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2013
000139657 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1385038903_32292
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000139657 520__ $$aSrc homology 3 (SH3) domains are widely known for their ability to interact with other proteins using the canonical PxxP binding motif. Besides those well-characterized interaction modes, there is an increasing number of SH3 domain-containing complexes that lack this motif. Here we characterize the interaction of SH3 domains, in particular the Bin1-SH3 domain, with the intrinsically disordered part of nonstructural protein 5A of the hepatitis C virus using noncanonical binding sites in addition to its PxxP motif. These binding regions partially overlap with regions that have previously been identified as having an increased propensity to form α-helices. Remarkably, upon interaction with the Bin1-SH3 domain, the α-helical propensity decreases and a fuzzy complex is formed.
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000139657 7001_ $$0P:(DE-HGF)0$$aSolyom, Z.$$b1
000139657 7001_ $$0P:(DE-HGF)0$$aFeuerstein, S.$$b2
000139657 7001_ $$0P:(DE-Juel1)131990$$aAladag, Amine$$b3$$ufzj
000139657 7001_ $$0P:(DE-Juel1)132003$$aHoffmann, Silke$$b4$$ufzj
000139657 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b5$$ufzj
000139657 7001_ $$0P:(DE-HGF)0$$aBrutscher, B.$$b6
000139657 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi400363v$$p6160-6168$$tBiochemistry$$v52$$x1520-4995
000139657 8564_ $$uhttp://pubs.acs.org/doi/abs/10.1021/bi400363v
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