%0 Journal Article
%A Schwarten, Melanie
%A Solyom, Z.
%A Feuerstein, S.
%A Aladag, Amine
%A Hoffmann, Silke
%A Willbold, Dieter
%A Brutscher, B.
%T Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites
%J Biochemistry
%V 52
%@ 1520-4995
%C Columbus, Ohio
%I American Chemical Society
%M FZJ-2013-05635
%P 6160-6168
%D 2013
%X Src 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000330099900004
%R 10.1021/bi400363v
%U https://juser.fz-juelich.de/record/139657