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| 001 | 139657 | ||
| 005 | 20210129212638.0 | ||
| 024 | 7 | _ | |a 10.1021/bi400363v |2 doi |
| 024 | 7 | _ | |2 WOS |a WOS:000330099900004 |
| 037 | _ | _ | |a FZJ-2013-05635 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Schwarten, Melanie |0 P:(DE-Juel1)132019 |b 0 |u fzj |e Corresponding author |
| 245 | _ | _ | |a Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites |
| 260 | _ | _ | |a Columbus, Ohio |c 2013 |b American Chemical Society |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1385038903_32292 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 520 | _ | _ | |a 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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| 700 | 1 | _ | |a Solyom, Z. |0 P:(DE-HGF)0 |b 1 |
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| 700 | 1 | _ | |a Brutscher, B. |0 P:(DE-HGF)0 |b 6 |
| 773 | _ | _ | |a 10.1021/bi400363v |p 6160-6168 |0 PERI:(DE-600)1472258-6 |t Biochemistry |v 52 |x 1520-4995 |
| 856 | 4 | _ | |u http://pubs.acs.org/doi/abs/10.1021/bi400363v |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/139657/files/FZJ-2013-05635.pdf |y Restricted |
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