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 08-22-2010, 03:29 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,589
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 NMR studies delineating spatial relationships within the cardiac troponin I-troponin

NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex.

Related Articles NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex.

J Biol Chem. 1994 Sep 23;269(38):23731-5

Authors: Krudy GA, Kleerekoper Q, Guo X, Howarth JW, Solaro RJ, Rosevear PR

NMR spectroscopy and selective isotope labeling of both recombinant cardiac troponin C (cTnC3) and a truncated cardiac troponin I (cTnI/NH2) lacking the N-terminal 32-amino acid cardiac-specific sequence have been used to probe protein-protein interactions central to muscle contraction. Using [methyl-13C]Met-labeled cTnC3, all 10 cTnC Met residues of Ca(2+)-saturated cTnC3 could be resolved in the two-dimensional heteronuclear single- and multiple-quantum coherence spectrum of the cTnI.cTnC complex. Based on the known Met assignments in cTnC3, the largest chemical shift changes were observed for Met81, Met120, Met137, and Met157. Methionines 120, 137, and 157 are all located in the C-terminal domain of cTnC. Methionine 81 is located at the N terminus of the central helix. Minimal chemical shift changes were observed for Met45, Met47, and Met103 of cTnC3 in the cTnI.cTnC complex. All 6 Met residues in [methyl13C]Met-labeled cTnI/NH2 could be resolved in the cTnI.cTnC complex, suggesting that both cTnI and cTnC form a stable homogeneous binary complex under the conditions of the NMR experiment. In the absence of added protease inhibitors in the cTnI.cTnC complex, cTnI/NH2 was found to undergo selective proteolysis to yield a 5.5-kDa N-terminal fragment corresponding to residues 33-80. Judging from the NMR spectra of [methyl13C]Met-labeled cTnC3, cTnI-(33-80) was sufficient for interaction with the C-terminal domain of cTnC in a manner identical to that observed for native cTnI/NH2. However, in the presence of the proteolytic fragment cTnI-(33-80), the chemical shift of Met81 was not perturbed from its position in free cTnC3. Thus, residues located C-terminal to Arg80 in cTnI appear to be responsible for interaction with the N-terminal half of cTnC. Taken together, these results provide strong evidence for an antiparallel arrangement for the two proteins in the troponin complex such that the N-terminal portion of cTnI interacts with the C-terminal domain of cTnC. This interaction likely plays a role in maintaining the stability of the TnI.TnC complex.

PMID: 8089144 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies.
Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies. Related Articles Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies. Protein Sci. 2005 Sep;14(9):2447-60 Authors: Wang X, Mercier P, Letourneau PJ, Sykes BD 19F NMR spectroscopy is potentially a powerful tool for...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-N
The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study. Related Articles The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study. FEBS Lett. 2002 Feb 27;513(2-3):289-93 Authors: Schmidtmann A, Lohmann K, Jaquet K Cardiac troponin I, the inhibitory subunit of the heterotrimeric cardiac troponin (cTn) complex is phosphorylated by protein kinase A at two serine residues located in its heart-specific N-terminal extension. This flexible arm interacts at different sites...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Cardiac troponin I induced conformational changes in cardiac troponin C as monitored
Cardiac troponin I induced conformational changes in cardiac troponin C as monitored by NMR using site-directed spin and isotope labeling. Related Articles Cardiac troponin I induced conformational changes in cardiac troponin C as monitored by NMR using site-directed spin and isotope labeling. Biochemistry. 1995 Oct 17;34(41):13343-52 Authors: Kleerekoper Q, Howarth JW, Guo X, Solaro RJ, Rosevear PR Conformational changes in both free cardiac troponin C (cTnC) and in complex with a recombinant troponin I protein were observed by means of a...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calci
Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Related Articles Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Biochemistry. 1991 Oct 22;30(42):10236-45 Authors: Brito RM, Putkey JA, Strynadka NC, James MN, Rosevear PR One- and two-dimensional NMR techniques were used to study both the influence of mutations on the structure of recombinant normal cardiac troponin C (cTnC3) and the conformational changes induced by Ca2+ binding to site II,...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calci
Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Related Articles Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Biochemistry. 1991 Oct 22;30(42):10236-45 Authors: Brito RM, Putkey JA, Strynadka NC, James MN, Rosevear PR One- and two-dimensional NMR techniques were used to study both the influence of mutations on the structure of recombinant normal cardiac troponin C (cTnC3) and the conformational changes induced by Ca2+ binding to site II,...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhib
Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C. Related Articles Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C. Biochem Cell Biol. 1991 Sep;69(9):674-81 Authors: Campbell AP, Cachia PJ, Sykes BD We have used 19F nuclear magnetic resonance spectroscopy to study the interaction of the inhibitory region of troponin (TnI) with apo- and calcium(II)-saturated turkey...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhib
Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C. Related Articles Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C. Biochem Cell Biol. 1991 Sep;69(9):674-81 Authors: Campbell AP, Cachia PJ, Sykes BD We have used 19F nuclear magnetic resonance spectroscopy to study the interaction of the inhibitory region of troponin (TnI) with apo- and calcium(II)-saturated turkey...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation.
NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation. FEBS Lett. 1999 Jun 18;453(1-2):107-12 Authors: Finley N, Abbott MB, Abusamhadneh E, Gaponenko V, Dong W, Gasmi-Seabrook G, Howarth JW, Rance M, Solaro RJ, Cheung HC, Rosevear PR Phosphorylation of the cardiac specific amino-terminus of troponin I has...
nmrlearner Journal club 0 08-21-2010 04:03 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 - 2017, 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 08:06 AM.


Map