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.

		BioNMR > Educational resources > Journal club
[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.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

12-11-2014, 11:22 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

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 based on NMR spectroscopy, of the intrinsically disordered C-terminal domain of the Nipah virus nucleoprotein (NTAIL ), both in its isolated state and within the nucleocapsid (NC). Within the NC the second half of NTAIL retains conformational behavior similar to that of isolated NTAIL , whereas the first half of NTAIL becomes much more rigid. In spite of the mostly disordered nature of NTAIL , chemical shifts and relaxation measurements show a significant degree of ?-helical sampling in the molecular recognition element (MoRE) involved in binding to the X domain (XD) of the phosphoprotein, with this preconfiguration being more pronounced than in the NTAIL domain from the cognate Hendra virus. Outside the MoRE, an additional region exhibiting reduced flexibility was identified within NTAIL and found to be involved in binding to the XD. (1) H- and (13) C-detected titration NMR experiments support a highly dynamic binding of NTAIL at the surface of the XD.

PMID: 25492314 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos Role of Electrostatic Interactions in Binding of Peptidesand Intrinsically Disordered Proteins to Their Folded Targets. 1.NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the PeptideSos http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500904f/20141007/images/medium/bi-2014-00904f_0012.gif Biochemistry DOI: 10.1021/bi500904f http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/uw_59WsXyRU More...	nmrlearner	Journal club	0	10-08-2014 04:17 AM
[NMR paper] The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. Related Articles The role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between c-Crk N SH3 domain and peptide Sos. Biochemistry. 2014 Sep 10; Authors: Xue Y, Yuwen T, Zhu F, Skrynnikov NR Abstract ...	nmrlearner	Journal club	0	09-11-2014 02:54 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...	nmrlearner	Journal club	0	08-14-2013 05:24 PM
[NMR paper] 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. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles NMR Determines Transient Structure and Dynamics in the Disordered C-Terminal Domain of WASp Interacting Protein. Biophys J. 2013 Jul 16;105(2):481-93 Authors: Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH Abstract WASp-interacting protein (WIP) is a 503-residue...	nmrlearner	Journal club	0	07-23-2013 09:52 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 , JordanH. Chill</br> WASp-interacting protein (WIP) is a 503-residue proline-rich polypeptide expressed in human Tcells. The WIP C-terminal domain binds to Wiskott-Aldrich syndrome protein (WASp) and regulates its activation and degradation, and the WIP-WASp...	nmrlearner	Journal club	0	07-16-2013 09:04 PM
[NMR paper] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy. Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy. Related Articles Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy. Chembiochem. 2013 Jun 6; Authors: Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M Abstract Intrinsically disordered regions (IDRs) are preferred sites for post-translational modifications essential for regulating protein function. The enhanced local...	nmrlearner	Journal club	0	06-08-2013 02:18 PM
Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP Quantitative Analysisof Multisite Protein–LigandInteractions by NMR: Binding of Intrinsically Disordered p53 TransactivationSubdomains with the TAZ2 Domain of CBP Munehito Arai, Josephine C. Ferreon and Peter E. Wright http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209936u/aop/images/medium/ja-2011-09936u_0012.gif Journal of the American Chemical Society DOI: 10.1021/ja209936u http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/ak4BxkITHl8	nmrlearner	Journal club	0	02-16-2012 05:24 AM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomol NMR Assign. 2011 Jun 7; Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...	nmrlearner	Journal club	0	06-08-2011 11:30 AM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off