[NMR paper] Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1H?-detected NMR measurements
Protein p53 is mostly known for playing a key role in tumour suppression, and mutations in the p53 gene are amongst the most frequent genomic events accompanying oncogenic transformation. Continuous research is conducted to target disordered proteins/protein regions for cancer therapy, for which atomic level information is also necessary. The disordered N-terminal part of p53 contains the transactivation and the proline-rich domains-which besides being abundant in proline residues-contains...
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
Abstract
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for regulation of C-H1.0 function. Since C-H1.0 is an intrinsically disordered domain, solution NMR is an excellent approach to characterize the...
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11-25-2018 06:02 AM
[NMR paper] Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
Sensitivity-enhanced Four-dimensional Amide-amide Correlation NMR Experiments for Sequential Assignment of Proline-rich Disordered Proteins.
J Am Chem Soc. 2018 Feb 28;:
Authors: Wong LE, Maier J, Wienands J, Becker S, Griesinger C
Abstract
Proline is prevalent in intrinsically disordered proteins (IDPs). NMR assignment of proline-rich IDPs is a challenge due to low dispersion of chemical...
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03-01-2018 09:20 PM
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00618/20170823/images/medium/bi-2017-006182_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00618
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08-24-2017 08:38 AM
[NMR paper] Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Related Articles Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Chembiochem. 2014 Dec 9;
Authors: Baronti L, Erales J, Habchi J, Felli IC, Pierattelli R, Longhi S
Abstract
We provide an atomic-resolution description...
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12-11-2014 11:22 PM
[NMR paper] Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Sci Rep. 2013;3:2913
Authors: Ogura K, Okamura H
Abstract
Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The...
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10-10-2013 09:38 PM
NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein
NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein
Publication date: 16 July 2013
Source:Biophysical Journal, Volume 105, Issue 2</br>
Author(s): Noam Y. Haba , Renana Gross , Jiri Novacek , Hadassa Shaked , Lukas Zidek , Mira Barda-Saad , Jordan*H. Chill</br>
WASp-interacting protein (WIP) is a 503-residue proline-rich polypeptide expressed in human T*cells. The WIP C-terminal domain binds to Wiskott-Aldrich syndrome protein (WASp) and regulates its activation and degradation, and the WIP-WASp...
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07-16-2013 09:04 PM
[NMR paper] NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-ric
NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos.
Related Articles NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos.
Nat Struct Biol. 1994 Dec;1(12):898-907
Authors: Goudreau N, Cornille F, Duchesne M, Parker F, Tocqué B, Garbay C, Roques BP
GRB2 is a small adaptor protein of 217 amino acids comprising one SH2 domain surrounded by two SH3 domains. GRB2 couples receptor tyrosine kinase activation to Ras signalling by interacting,...
Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1H?-detected NMR measurements
Linear Mode
