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 11-17-2010, 11:15 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,700
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 Metal ion binding to calmodulin: NMR and fluorescence studies.

Metal ion binding to calmodulin: NMR and fluorescence studies.

Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.

Biometals. 1998 Sep;11(3):213-22

Authors: Ouyang H, Vogel HJ

Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad specificity for binding metal ions. Using 15N-Gly biosynthetically-labelled calmodulin, we have studied the binding of different metal ions to calmodulin, including K+, Na+, Ca2+, Mg2+, Zn2+, Cd2+, Pb2+, Hg2+, Sr2+, La3+ and Lu3+, by 1H,15N HMQC NMR experiments. The effects of these ions on the substrate-binding ability of calmodulin have also been studied by fluorescence spectroscopy of the single tryptophan residue in a 22-residue synthetic peptide encompassing the skeletal muscle myosin light chain kinase calmodulin-binding domain. Most of these metal ions can activate a calmodulin target enzyme to some extent, though they bind to calmodulin in a different manner. Mg2+, which is of direct physiological interest, has a distinct site-preference for calmodulin, as it shows the highest affinity for site I in the N-terminal domain, while the C-terminal sites III and IV are the high affinity binding sites for Ca2+ (as well as for Cd2+). At a high concentration of Mg2+ and a low concentration of Ca2+, calmodulin can bind Mg2+ in its N-terminal lobe while the C-terminal domain is occupied by Ca2+; this species could exist in resting cells in which the Mg2+ level significantly exceeds that of Ca2+. Moreover, our data suggest that the toxicity of Pb(2+)--which, like Sr2+, binds with an equal and high affinity to all four sites--may be related to its capacity to tightly bind and improperly activate calmodulin.

PMID: 9850564 [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, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein.
NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein. NMR, biophysical and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein. J Biol Chem. 2011 Jul 28; Authors: Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1) infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein...
nmrlearner Journal club 0 07-30-2011 11:23 AM
[NMR paper] Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubu
Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods. Related Articles Effect of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin studied by fluorescence and NMR spectroscopic methods. Physiol Chem Phys Med NMR. 2001;33(2):139-51 Authors: Kuchroo K, Maity H, Kasturi SR Tubulin, the major protein of microtubules, has been shown to be an example of protein undergoing multistep unfolding. Local unfolding and stepwise loss of a...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9. Related Articles NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9. J Inorg Biochem. 2000 Apr;79(1-4):365-70 Authors: Hannan JP, Whittaker SB, Hemmings AM, James R, Kleanthous C, Moore GR The 134 amino acid DNase domain of colicin E9 contains a zinc-finger-like HNH motif that binds divalent transition metal ions. We have used 1D 1H and 2D 1H-15N NMR methods to characterise the binding of Co2+, Ni2+ and Zn2+ to this protein. Data for the...
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] [13C]Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe
Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Related Articles Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Biochem J. 1999 Dec 15;344 Pt 3:881-7 Authors: He QY, Mason AB, Tam BM, MacGillivray RT, Woodworth RC The N-lobe of human serum transferrin (hTF/2N) and single point mutants in which each...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lip
1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex. FEBS Lett. 1997 Oct 20;416(2):130-4 Authors: Sodano P, Caille A, Sy D, de Person G, Marion D, Ptak M Plant non-specific lipid transfer proteins (LTPs) are...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins.
NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins. Related Articles NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins. Biochim Biophys Acta. 1996 Mar 7;1293(1):72-82 Authors: Aramini JM, Hiraoki T, Grace MR, Swaddle TW, Chiancone E, Vogel HJ 1H-NMR spectroscopy and stopped-flow techniques have been used to investigate the binding of a host of metal ions to alpha-lactalbumins from bovine, goat, and human sources. We have identified two 1H-NMR markers diagnostic of metal ion binding to the...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein. Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein. Biochemistry. 1994 Jan 11;33(1):65-73 Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein. Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein. Biochemistry. 1994 Jan 11;33(1):65-73 Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
nmrlearner Journal club 0 08-22-2010 03:33 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 01:55 PM.


Map