BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 11-09-2015, 02:00 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,777
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.

Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.

Related Articles Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.

J Mol Biol. 2015 Oct 29;

Authors: Clark MD, Zhang Y, Radhakrishnan I

Abstract
The Sds3 transcriptional corepressor facilitates the assembly of the 1-2 megadalton histone deacetylase (HDAC)-associated Sin3L/Rpd3L complex by providing a crucial homo-dimerization activity. Sds3 engages the scaffolding protein Sin3A, via a bipartite motif within the Sin3 interaction domain (SID) comprising a helix and an extended segment. Here we show that the SID samples two discrete, substantially populated conformations with lifetimes in the tens of milliseconds range. The two conformations differ via a translation of the main chain and the corresponding side chains in the 5 to 7Å range. Given the close proximity of the SID to other functional motifs in Sds3 at the sequence level, the conformational exchange has the potential to regulate these activities.


PMID: 26522936 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH
From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The bibliography manager for researchers
nmrlearner Journal club 0 09-29-2015 02:39 PM
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. 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 Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH. Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7 Authors: Werbeck ND, Kirkpatrick J,...
nmrlearner Journal club 0 01-29-2014 02:01 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH
From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The reference manager for researchers
nmrlearner Journal club 0 10-17-2013 12:49 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH
From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The reference manager for researchers
nmrlearner Journal club 0 04-11-2013 09:27 PM
[NMR paper] Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH
From Mendeley Biomolecular NMR group: Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH Angewandte Chemie International Edition (2013). Pages: n/a-n/a. Nicolas D. Werbeck, John Kirkpatrick, D. Flemming Hansen et al. Published using Mendeley: The library management tool for researchers
nmrlearner Journal club 0 04-11-2013 03:08 PM
Bacillus subtilis deletion strains studied by 23Na NMR reveal that the antiporter-subunit MrpA and the complex I subunit NuoL are Na+-transporter proteins
Bacillus subtilis deletion strains studied by 23Na NMR reveal that the antiporter-subunit MrpA and the complex I subunit NuoL are Na+-transporter proteins October 2012 Publication year: 2012 Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics, Volume 1817, Supplement</br> </br> </br> </br></br>
nmrlearner Journal club 0 02-03-2013 10:13 AM
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time. NMR profiling of histone deacetylase and acetyl-transferase activities in real time. ACS Chem Biol. 2011 May 20;6(5):419-24 Authors: Dose A, Liokatis S, Theillet FX, Selenko P, Schwarzer D Abstract Histone deacetylases (HDACs) and histone acetyl-transferases (HATs) are universal regulators of eukaryotic transcriptional activity and emerging therapeutic targets for human diseases. Here we describe the generation of isotope-labeled deacetylation and...
nmrlearner Journal club 0 09-07-2011 06:28 PM
[NMR paper] Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [
Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan. Related Articles Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan. J Biomol NMR. 1995 Jun;5(4):367-75 Authors: Lee W, Revington M, Farrow NA, Nakamura A, Utsunomiya-Tate N, Miyake Y, Kainosho M, Arrowsmith CH -L-tryptophan was prepared biosynthetically and its dynamic properties and intermolecular interaction with a complex of Escherichia coli trp-repressor and a 20 base-pair operator DNA were...
nmrlearner Journal club 0 08-22-2010 03:41 AM



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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 03:39 PM.


Map