[NMR paper] Model of the Interaction between the NF-?B Inhibitory protein p100 and the E3 ubiquitin ligase ?-TrCP based on NMR and Docking Experiments.
Related ArticlesModel of the Interaction between the NF-?B Inhibitory protein p100 and the E3 ubiquitin ligase ?-TrCP based on NMR and Docking Experiments.
J Chem Inf Model. 2016 Dec 22;:
Authors: Melikian M, Eluard B, Bertho G, Baud V, Evrard-Todeschi N
Abstract
NF-?B is a major transcription factor whose activation is triggered through two main activation pathways: the canonical pathway involving disruption of I?B-?/NF-?B complexes and the alternative pathway whose activation relies on the inducible proteolysis of the inhibitory protein p100. One central step controlling p100 processing consists in the interaction of the E3 ubiquitin ligase ?-TrCP with p100, thereby leading to its ubiquitinylation and subsequent either complete degradation or partial proteolysis by the proteasome. However, the interaction mechanism between p100 and ?-TrCP is still poorly defined. In this work, a diphosphorylated 21-mer p100 peptide model containing the phosphodegron motif was used to characterize the interaction with ?-TrCP by NMR. In parallel, docking simulations were performed in order to obtain a model of the 21P-p100/ ?-TrCP complex. STD experiments were performed in order to highlight the residues of p100 involved in the interaction with the ?-TrCP protein. These results highlighted the importance of pSer865 and pSer869 residues in the interaction with ?-TrCP and particularly the Tyr867 that fits inside the hydrophobe ?-TrCP cavity with the Arg474 guanidinium group. Four other arginines, Arg285, Arg410, Arg431, and Arg521 were found essential in the stabilization of p100 on the ?-TrCP surface. Importantly, the requirement for these five arginine residues of ?-TrCP for the interaction with p100 was further confirmed in vivo, thereby validating the docking model through a biological approach.
PMID: 28004927 [PubMed - as supplied by publisher]
Apoptosis Inducing Factor Binding Protein PGAM5 TriggersMitophagic Cell Death That Is Inhibited by the Ubiquitin Ligase Activityof X-Linked Inhibitor of Apoptosis
Apoptosis Inducing Factor Binding Protein PGAM5 TriggersMitophagic Cell Death That Is Inhibited by the Ubiquitin Ligase Activityof X-Linked Inhibitor of Apoptosis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00306/20160601/images/medium/bi-2016-003067_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00306
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/B9hzsL2NEXs
More...
nmrlearner
Journal club
0
06-03-2016 03:35 AM
[NMR paper] On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
Related Articles On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking.
J Chem Inf Model. 2015 Jul 30;
Authors: Onila I, Ten Brink T, Fredriksson K, Codutti L, Mazur A, Griesinger C, Carlomagno T, Exner TE
Abstract
INPHARMA (Internuclear NOEs for Pharmacophore Mapping) determines the relative orientation of two competitive ligands in the protein binding pocket. It is based on the...
nmrlearner
Journal club
0
08-02-2015 07:10 AM
[NMR paper] NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
Biopolymers. 2013 Sep 4;
Authors: Heisel KA, Krishnan VV
...
nmrlearner
Journal club
0
09-17-2013 11:36 PM
Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A
Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A
Abstract Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling degradation of p53. This article describe the solution NMR structure of the conserved N-terminal domain of human Ube3A (residues 24-87) that contains two residues (Cys44 and Arg62) found to be mutated in patients with Angelman syndrome. The structure of this domain...
nmrlearner
Journal club
0
09-30-2011 08:01 PM
[NMR paper] Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Related Articles Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Proteins. 2005 Aug 15;60(3):367-81
Authors: van Dijk AD, Fushman D, Bonvin AM
When classical, Nuclear Overhauser Effect (NOE)-based approaches fail, it is possible, given high-resolution...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.
Related Articles NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.
J Biol Chem. 2004 Jul 23;279(30):31455-61
Authors: Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H
A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Related Articles Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Anal Chem. 2003 Feb 15;75(4):956-60
Authors: Kakuta M, Jayawickrama DA, Wolters AM, Manz A, Sweedler JV
Time-resolved NMR spectroscopy is used to studychanges in protein conformation based on the elapsed time after a change in the solvent composition of a protein solution. The use of a micromixer and a continuous-flow method is described where the contents of...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Structure prediction of protein complexes by an NMR-based protein docking algorithm.
Structure prediction of protein complexes by an NMR-based protein docking algorithm.
Related Articles Structure prediction of protein complexes by an NMR-based protein docking algorithm.
J Biomol NMR. 2001 May;20(1):15-21
Authors: Kohlbache O, Burchardt A, Moll A, Hildebrandt A, Bayer P, Lenhof HP
Protein docking algorithms can be used to study the driving forces and reaction mechanisms of docking processes. They are also able to speed up the lengthy process of experimental structure elucidation of protein complexes by proposing potential...
Model of the Interaction between the NF-?B Inhibitory protein p100 and the E3 ubiquitin ligase ?-TrCP based on NMR and Docking Experiments.
Linear Mode
