TY  - JOUR
AU  - Schwarten, Melanie
AU  - Solyom, Z.
AU  - Feuerstein, S.
AU  - Aladag, Amine
AU  - Hoffmann, Silke
AU  - Willbold, Dieter
AU  - Brutscher, B.
TI  - Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites
JO  - Biochemistry
VL  - 52
SN  - 1520-4995
CY  - Columbus, Ohio
PB  - American Chemical Society
M1  - FZJ-2013-05635
SP  - 6160-6168
PY  - 2013
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000330099900004
DO  - DOI:10.1021/bi400363v
UR  - https://juser.fz-juelich.de/record/139657
ER  -