Conserved homology 1 (C1) domains are peripheral zinc finger domains that are responsible for recruiting their host signaling proteins, including Protein Kinase C (PKC) isoenzymes, to diacylglycerol-containing lipid membranes. In this work, we investigated the reactivity of the C1 structural zinc sites, using the cysteine-rich C1B regulatory region of the PKC? isoform as a paradigm. The choice of Cd^(2+) as a probe was prompted by previous findings that xenobiotic metal ions modulate PKC...
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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[ASAP] The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00572/20180626/images/medium/bi-2018-00572h_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00572
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06-27-2018 01:51 AM
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] Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.
Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.
Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Apr 2;
Authors: Chen Y, Zhang Z, Tang X, Li J, Glaubitz C, Yang J
Abstract
Solid-state NMR is a powerful tool for studying membrane proteins in a native-like lipid environment. 3D magic angle spinning (MAS) NMR was employed to characterize the structure of E.coli diacylglycerol...
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04-06-2014 02:01 AM
[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 paper] Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Chemistry. 2013 Aug 12;
Authors: Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone EM, Fattorusso R
Abstract
Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with...
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08-14-2013 05:24 PM
[NMR paper] NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli Dna
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
J Mol Biol. 1996 Jul 12;260(2):236-50
Authors: Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K
The recombinant N-terminal 107-amino acid polypeptide fragment 2-108 of the DnaJ molecular chaperone of Escherichia...
Reactivity of Thiol-Rich Zn Sites in Diacylglycerol-Sensing PKC C1 Domain Probed by NMR Spectroscopy
Linear Mode
