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



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  
Unread 10-12-2017, 01:25 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 Detailed Evidence for an Unparalleled Interaction Mode between Calmodulin and Orai Proteins

Detailed Evidence for an Unparalleled Interaction Mode between Calmodulin and Orai Proteins


Calmodulin (CaM) binds most of its targets by wrappingaround an amphipathic ?-helix. The N-terminus of Orai proteins contains a conserved CaM-binding segment but the binding mechanism is only partially characterized. Here, microscale thermophoresis (MST), surface plasmon resonance (SPR), andatomic force microscopy (AFM) were employed to study the binding equilibria, the kinetics, and the single-molecular interaction forces involved in the binding of CaM to the conserved helical segments of Orai1 and Orai3. The results consistently indicated step-wise binding of two separate target peptides to the two lobes of CaM. An unparalleled high affinity was found when two Orai peptides were dimerized or immobilized at high lateral density, thereby mimicking the close proximity of the N-termini in native Orai oligomers. The analogous experiments with smooth muscle myosin light chain kinase (smMLCK) showed only the expected 1:1 binding, confirming the validity of our methods.

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange.
Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange. Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange. Angew Chem Int Ed Engl. 2017 Aug 28;: Authors: Gao J, Liang E, Ma R, Li F, Liu Y, Liu J, Jiang L, Li C, Dai H, Wu J, Su X, He W, Ruan K Abstract The characterization of protein-ligand interaction modes becomes recalcitrant in the NMR intermediate exchange regime as the...
nmrlearner Journal club 0 08-29-2017 05:35 PM
[NMR paper] Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange
Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange The characterization of protein-ligand interaction modes becomes recalcitrant in the NMR intermediate exchange regime as the interface resonances are broadened beyond detection. Here, we determined the 19F low-populated bound-state pseudocontact shifts (PCSs) of mono- and di-fluorinated inhibitors of the BRM bromodomain using a highly-skewed protein/ligand ratio. The bound-state 19F PCSs were retrieved from 19F chemical exchange saturation transfer (CEST) in...
nmrlearner Journal club 0 08-29-2017 01:33 AM
Mode of Interaction of the Signal-Transducing ProteinEIIAGlc with the Maltose ABC Transporter in the Processof Inducer Exclusion
Mode of Interaction of the Signal-Transducing ProteinEIIAGlc with the Maltose ABC Transporter in the Processof Inducer Exclusion http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00721/20160919/images/medium/bi-2016-007219_0007.gif Biochemistry DOI: 10.1021/acs.biochem.6b00721 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/OA3oK_Ae-hI More...
nmrlearner Journal club 0 09-22-2016 06:22 AM
Free-electron lasers reveal detailed architecture of proteins - R & D Magazine
Free-electron lasers reveal detailed architecture of proteins - R & D Magazine http://www.bionmr.com//nt1.ggpht.com/news/tbn/1ed-82XzQnyMGM/6.jpg R & D Magazine <img alt="" height="1" width="1" /> Free-electron lasers reveal detailed architecture of proteins R & D Magazine An international team of researchers has recently analyzed protein crystals using ... of a new 0.75-mm solid state nuclear magnetic resonance (NMR) probe. and more &raquo;
nmrlearner Online News 0 06-13-2012 11:34 AM
NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin.
NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin. NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin. Biochim Biophys Acta. 2011 May 24; Authors: Chen AS, Kim YM, Gayen S, Huang Q, Raida M, Kang C The serotonin (5-HT(1A)) receptor, a G-protein-coupled receptor (GPCR), plays important roles in serotonergic signaling in the central nervous system. The third intracellular loop (ICL3) of the 5-HT(1A) receptor has...
nmrlearner Journal club 0 06-07-2011 11:05 AM
[NMR paper] NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin. Related Articles NMR and molecular dynamics studies of the interaction of melatonin with calmodulin. Protein Sci. 2004 Nov;13(11):2925-38 Authors: Turjanski AG, Estrin DA, Rosenstein RE, McCormick JE, Martin SR, Pastore A, Biekofsky RR, Martorana V Pineal hormone melatonin (N-acetyl-5-methoxytryptamine) is thought to modulate the calcium/calmodulin signaling pathway either by changing intracellular Ca(2+) concentration via activation of its G-protein-coupled...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] 13C NMR study of the mode of interaction in solution of the B fragment of staphylococ
13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G. FEBS Lett. 1993 Aug 9;328(1-2):49-54 Authors: Kato K, Gouda H, Takaha W, Yoshino A, Matsunaga C, Arata Y The mode of interaction of...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H
Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy. Related Articles Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy. Biochim Biophys Acta. 1992 Nov 10;1160(1):22-34 Authors: Gao Y, Levine BA, Mornet D, Slatter DA, Strasburg GM In order to identify comparative aspects of the interaction of calmodulin with its target proteins, proton magnetic-resonance studies of complex formation between calmodulin and defined segments of phospholamban...
nmrlearner Journal club 0 08-21-2010 11:45 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



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 02:34 AM.


Map