NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II

The Hepatitis C Virus (HCV)11 HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; CSP: combined chemical shift perturbations; THP...

Full description

Bibliographic Details
Main Authors: Luiza M. Bessa, Robert Schneider, Xavier Hanoulle
Format: Article
Language:English
Published: Elsevier 2018-04-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340918300416
_version_ 1818328239672655872
author Luiza M. Bessa
Robert Schneider
Xavier Hanoulle
author_facet Luiza M. Bessa
Robert Schneider
Xavier Hanoulle
author_sort Luiza M. Bessa
collection DOAJ
description The Hepatitis C Virus (HCV)11 HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; CSP: combined chemical shift perturbations; THP: (Tris(hydroxypropyl)phosphine). nonstructural 5A protein (NS5A) is a phosphoprotein (Evans et al., 2004; Ross-Thriepland and Harris, 2014) [1,2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains (Moradpour et al., 2007; Bartenschlager et al., 2013; Badillo et al., 2017) [3–5]. So far, no precise molecular function has been identified for this viral protein (Ross-Thriepland and Harris, 2015) [6] which is required for viral replication (Tellinghuisen et al., 2008) [7]. In this article, we present datasets of NMR and circular dichroism analyses of the domain 2 of the HCV NS5A protein (NS5A-D2) phosphorylated in vitro by the Casein Kinase II (CKII) (Dal Pero et al., 2007; Clemens et al., 2015; Masak et al., 2014; Kim et al., 2014) [8–11]. We describe the in vitro phosphorylation of the serine 288 (pS288) of NS5A-D2 by CKII and report the circular dichroism spectrum of the phosphorylated domain (NS5-D2_CKII). This data article also contains the 1H, 15N and 13C NMR chemical shift assignments (HN, N, Cα, Cβ and C’) for the phosphorylated NS5A-D2 domain, and an assigned 1H,15N-HSQC spectrum is shown. The NMR data have been acquired on an 800 MHz spectrometer. These NMR data have been used to calculate both the 1H,15N combined chemical shift perturbations (CSP) induced by the phosphorylation of pS288 and the secondary structural propensity (SSP) scores that describe the structural tendencies in this intrinsically disordered domain. The circular dichroism spectrum and the SSP scores of NS5A-D2_CKII have been compared with those of unphosphorylated NS5A-D2 [12,13]. Keywords: HCV NS5A, NMR, Phosphorylation, IDP
first_indexed 2024-12-13T12:29:00Z
format Article
id doaj.art-8f61fd7817e24761b6900e9653fa6996
institution Directory Open Access Journal
issn 2352-3409
language English
last_indexed 2024-12-13T12:29:00Z
publishDate 2018-04-01
publisher Elsevier
record_format Article
series Data in Brief
spelling doaj.art-8f61fd7817e24761b6900e9653fa69962022-12-21T23:46:07ZengElsevierData in Brief2352-34092018-04-0117325333NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase IILuiza M. Bessa0Robert Schneider1Xavier Hanoulle2University of Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, FranceUniversity of Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, FranceCorresponding authors. Phone: +33(0)362531716; University of Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, FranceThe Hepatitis C Virus (HCV)11 HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; CSP: combined chemical shift perturbations; THP: (Tris(hydroxypropyl)phosphine). nonstructural 5A protein (NS5A) is a phosphoprotein (Evans et al., 2004; Ross-Thriepland and Harris, 2014) [1,2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains (Moradpour et al., 2007; Bartenschlager et al., 2013; Badillo et al., 2017) [3–5]. So far, no precise molecular function has been identified for this viral protein (Ross-Thriepland and Harris, 2015) [6] which is required for viral replication (Tellinghuisen et al., 2008) [7]. In this article, we present datasets of NMR and circular dichroism analyses of the domain 2 of the HCV NS5A protein (NS5A-D2) phosphorylated in vitro by the Casein Kinase II (CKII) (Dal Pero et al., 2007; Clemens et al., 2015; Masak et al., 2014; Kim et al., 2014) [8–11]. We describe the in vitro phosphorylation of the serine 288 (pS288) of NS5A-D2 by CKII and report the circular dichroism spectrum of the phosphorylated domain (NS5-D2_CKII). This data article also contains the 1H, 15N and 13C NMR chemical shift assignments (HN, N, Cα, Cβ and C’) for the phosphorylated NS5A-D2 domain, and an assigned 1H,15N-HSQC spectrum is shown. The NMR data have been acquired on an 800 MHz spectrometer. These NMR data have been used to calculate both the 1H,15N combined chemical shift perturbations (CSP) induced by the phosphorylation of pS288 and the secondary structural propensity (SSP) scores that describe the structural tendencies in this intrinsically disordered domain. The circular dichroism spectrum and the SSP scores of NS5A-D2_CKII have been compared with those of unphosphorylated NS5A-D2 [12,13]. Keywords: HCV NS5A, NMR, Phosphorylation, IDPhttp://www.sciencedirect.com/science/article/pii/S2352340918300416
spellingShingle Luiza M. Bessa
Robert Schneider
Xavier Hanoulle
NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
Data in Brief
title NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
title_full NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
title_fullStr NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
title_full_unstemmed NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
title_short NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II
title_sort nmr and circular dichroism data for domain 2 of the hcv ns5a protein phosphorylated by the casein kinase ii
url http://www.sciencedirect.com/science/article/pii/S2352340918300416
work_keys_str_mv AT luizambessa nmrandcirculardichroismdatafordomain2ofthehcvns5aproteinphosphorylatedbythecaseinkinaseii
AT robertschneider nmrandcirculardichroismdatafordomain2ofthehcvns5aproteinphosphorylatedbythecaseinkinaseii
AT xavierhanoulle nmrandcirculardichroismdatafordomain2ofthehcvns5aproteinphosphorylatedbythecaseinkinaseii