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Updated: May 8, 2026

A Protocol for Analyzing Hepatitis C Virus Replication
Published on: June 26, 2014
Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical
Melanie Schwarten1, Zsófia Sólyom, Sophie Feuerstein
1Institut de Biologie Structurale, Université Grenoble 1 , 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
Abstract:
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.
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