NMR paper Detecting protein kinase recognition modes of calmodulin by residual dipolar coupling

		BioNMR > Educational resources > Journal club
[NMR paper] Detecting protein kinase recognition modes of calmodulin by residual dipolar coupling

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

11-24-2010, 08:58 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,734

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

Detecting protein kinase recognition modes of calmodulin by residual dipolar coupling

Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

Related Articles Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

Biochemistry. 2002 Oct 29;41(43):12899-906

Authors: Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M

Calmodulin-regulated serine/threonine kinases (CaM kinases) play crucial roles in Ca2+-dependent signaling transduction pathways in eukaryotes. Despite having a similar overall molecular architecture of catalytic and regulatory domains, CaM kinases employ different binding modes for Ca2+/CaM recruitment which is required for their activation. Here we present a residual dipolar coupling (RDC)-based NMR approach to characterizing the molecular recognition of CaM with five different CaM kinases. Our analyses indicate that CaM kinase I and likely IV use the same CaM binding mode as myosin light chain kinase (1-14 motif), distinct from those of CaM kinase II (1-10 motif) and CaM kinase kinase (1-16- motif). This NMR approach provides an efficient experimental guide for homology modeling and structural characterization of CaM-target complexes.

PMID: 12390014 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
The Use of Residual Dipolar Coupling in Studying Proteins by NMR. The Use of Residual Dipolar Coupling in Studying Proteins by NMR. The Use of Residual Dipolar Coupling in Studying Proteins by NMR. Top Curr Chem. 2011 Sep 28; Authors: Chen K, Tjandra N Abstract The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...	nmrlearner	Journal club	0	09-30-2011 06:00 AM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR. The Use of Residual Dipolar Coupling in Studying Proteins by NMR. The Use of Residual Dipolar Coupling in Studying Proteins by NMR. Top Curr Chem. 2011 Sep 28; Authors: Chen K, Tjandra N Abstract The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...	nmrlearner	Journal club	0	09-30-2011 05:59 AM
Determination of the Structures of Symmetric Protein Oligomers from NMR Chemical Shifts and Residual Dipolar Couplings Determination of the Structures of Symmetric Protein Oligomers from NMR Chemical Shifts and Residual Dipolar Couplings Nikolaos G. Sgourakis, Oliver F. Lange, Frank DiMaio, Ingemar Andre?, Nicholas C. Fitzkee, Paolo Rossi, Gaetano T. Montelione, Ad Bax and David Baker http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja111318m/aop/images/medium/ja-2010-11318m_0008.gif Journal of the American Chemical Society DOI: 10.1021/ja111318m http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...	nmrlearner	Journal club	0	04-06-2011 10:54 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins. Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins. Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins. J Am Chem Soc. 2011 Feb 2; Authors: Shi L, Traaseth NJ, Verardi R, Gustavsson M, Gao J, Veglia G Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the...	nmrlearner	Journal club	0	02-04-2011 11:34 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins Lei Shi, Nathaniel J. Traaseth, Raffaello Verardi, Martin Gustavsson, Jiali Gao and Gianluigi Veglia http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109080t/aop/images/medium/ja-2010-09080t_0003.gif Journal of the American Chemical Society DOI: 10.1021/ja109080t http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/Tu9H79dfKCk	nmrlearner	Journal club	0	02-03-2011 06:45 AM
[NMR paper] Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar c Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar couplings--an assessment of the interrelation of NMR restraints. Related Articles Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar couplings--an assessment of the interrelation of NMR restraints. J Biomol NMR. 2004 Jan;28(1):31-41 Authors: Jensen PR, Axelsen JB, Lerche MH, Poulsen FM We have examined how the hydrogen bond geometry in three different proteins is affected when structural restraints based on measurements of...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] Protein structural motif recognition via NMR residual dipolar couplings. Protein structural motif recognition via NMR residual dipolar couplings. Related Articles Protein structural motif recognition via NMR residual dipolar couplings. J Am Chem Soc. 2001 Feb 14;123(6):1222-9 Authors: Andrec M, Du P, Levy RM NMR residual dipolar couplings have great potential to provide rapid structural information for proteins in the solution state. This information even at low resolution may be used to advantage in proteomics projects that seek to annotate large numbers of gene products for entire genomes. In this paper, we...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immuno Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. Related Articles Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. J Biol Chem. 2000 May 26;275(21):16174-82 Authors: Gaul BS, Harrison ML, Geahlen RL, Burton RA, Post CB The immunoreceptor tyrosine-based activation motif (ITAM) plays a central role...	nmrlearner	Journal club	0	11-18-2010 09:15 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