NMR paper Sites phosphorylated in bovine cardiac troponin T and I. Characterization by 31P-NMR

		BioNMR > Educational resources > Journal club
[NMR paper] Sites phosphorylated in bovine cardiac troponin T and I. Characterization by 31P-NMR

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

08-21-2010, 11:04 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

Sites phosphorylated in bovine cardiac troponin T and I. Characterization by 31P-NMR

Sites phosphorylated in bovine cardiac troponin T and I. Characterization by 31P-NMR spectroscopy and phosphorylation by protein kinases.

Related Articles Sites phosphorylated in bovine cardiac troponin T and I. Characterization by 31P-NMR spectroscopy and phosphorylation by protein kinases.

Eur J Biochem. 1990 Jul 5;190(3):575-82

Authors: Swiderek K, Jaquet K, Meyer HE, Schächtele C, Hofmann F, Heilmeyer LM

Bovine cardiac troponin isolated in a highly phosphorylated form shows four 31P-NMR signals [Beier, N., Jaquet, K., Schnackerz, K. & Heilmeyer, L.M.G. Jr (1988) Eur. J. Biochem. 176, 327-334]. Troponin I, which contains phosphate covalently linked to serine-23 and/or -24 [Swiderek, K., Jaquet, K., Meyer, H. E. & Heilmeyer, L. M. G. Jr (1988) Eur. J. Biochem. 176, 335-342], shows three resonances. Mg2(+)-saturation of holotroponin shifts these troponin I resonances to higher fields. Direct binding of Mg2+ to the phosphate groups can be excluded. Both these serine residues of troponin I, 23 and 24, are substrates for cAMP- and cGMP-dependent protein kinases as well as for protein kinase C. Isolated bovine cardiac troponin T contains 1.5 mol phosphoserine/mol protein, indicating that minimally two serine residues are phosphorylated. One phosphoserine residue is located at the N-terminus. An additional phosphoserine is located in the C-terminal cyanogen bromide fragment, CN4, which contains covalently bound phosphate. Protein kinase C phosphorylates serine-194, thus demonstrating exposure of this residue on the surface of holotoponin.

PMID: 2373082 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

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] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy. Related Articles Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy. Int J Pept Protein Res. 1996 Apr;47(4):282-8 Authors: Katahira R, Flotow H, Thomas G, Nosaka AY An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...	nmrlearner	Journal club	0	08-22-2010 02:27 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] 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...	nmrlearner	Journal club	0	08-22-2010 03:29 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] 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

« 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