JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on May 3, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/19/16351    most recent
C200139200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kranz, J. K.
Right arrow Articles by Wand, A. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kranz, J. K.
Right arrow Articles by Wand, A. J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print March 19, 2002
J. Biol. Chem, 10.1074/jbc.C200139200
Submitted on March 7, 2002
Revised on March 18, 2002
Accepted on March 19, 2002

A direct test of the reductionist approach to structural studies of calmodulin activity: relevance of peptide models of target proteins

James K. Kranz, Eun K. Lee, Angus C. Nairn, and A. Joshua Wand

Dept. of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, PA 19104-6059

Corresponding Author: wand{at}mail.med.upenn.edu

Ca2+-saturated calmodulin (CaM) directly associates with and activates CaM-dependent protein kinase I (CaMKI) through interactions with a short sequence in its regulatory domain. Using heteronuclear NMR 13C-15N-1H correlation experiments, the backbone assignments were determined for CaM bound to a peptide (CaMKIp) corresponding to the CaM-binding sequence of CaMKI. A comparison of chemical shifts for free CaM with those of the CaM:CaMKIp complex indicate large differences throughout the CaM sequence. Using NMR techniques optimized for large proteins, backbone resonance assignments were also determined for CaM bound to the intact CaMKI enzyme. NMR spectra of CaM bound to either the CaMKI enzyme or peptide are virtually identical indicating that calmodulin is structurally indistinguishable when complexed to the intact kinase or the peptide CaM-binding domain. Chemical shifts of CaM bound to a peptide (smMLCKp ) corresponding to the calmodulin-binding domain of smooth muscle myosin light chain kinase are also compared to the CaM:CaMKI complexes. Chemical shifts can differentiate one complex from another, as well as bound versus free states of CaM. In this context, the observed similarity between CaM:CaMKI enzyme and peptide complexes is striking, indicating the peptide is an excellent mimetic for interaction of calmodulin with the CaMKI enzyme.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
D. S. Libich and G. Harauz
Backbone Dynamics of the 18.5 kDa Isoform of Myelin Basic Protein Reveals Transient {alpha}-Helices and a Calmodulin-Binding Site
Biophys. J., June 15, 2008; 94(12): 4847 - 4866.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhou, W. Yang, M. M. Lurtz, Y. Ye, Y. Huang, H.-W. Lee, Y. Chen, C. F. Louis, and J. J. Yang
Identification of the Calmodulin Binding Domain of Connexin 43
J. Biol. Chem., November 30, 2007; 282(48): 35005 - 35017.
[Abstract] [Full Text] [PDF]

Home page
 Sci SignalHome page
W. J. Chazin
The Impact of X-ray Crystallography and NMR on Intracellular Calcium Signal Transduction by EF-Hand Proteins: Crossing the Threshold from Structure to Biology and Medicine
Sci. Signal., May 29, 2007; 2007(388): pe27 - pe27.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Rainaldi, A. P. Yamniuk, T. Murase, and H. J. Vogel
Calcium-dependent and -independent Binding of Soybean Calmodulin Isoforms to the Calmodulin Binding Domain of Tobacco MAPK Phosphatase-1
J. Biol. Chem., March 2, 2007; 282(9): 6031 - 6042.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
I. Andre, T. Kesvatera, B. Jonsson, and S. Linse
Salt Enhances Calmodulin-Target Interaction
Biophys. J., April 15, 2006; 90(8): 2903 - 2910.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Xiong, Q. K. Kleerekoper, R. He, J. A. Putkey, and S. L. Hamilton
Sites on Calmodulin That Interact with the C-terminal Tail of Cav1.2 Channel
J. Biol. Chem., February 25, 2005; 280(8): 7070 - 7079.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
I. Andre, T. Kesvatera, B. Jonsson, K. S. Akerfeldt, and S. Linse
The Role of Electrostatic Interactions in Calmodulin-Peptide Complex Formation
Biophys. J., September 1, 2004; 87(3): 1929 - 1938.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
D. S. Libich, C. M.D. Hill, I. R. Bates, F. R. Hallett, S. Armstrong, A. Siemiarczuk, and G. Harauz
Interaction of the 18.5-kD isoform of myelin basic protein with Ca2+-calmodulin: Effects of deimination assessed by intrinsic Trp fluorescence spectroscopy, dynamic light scattering, and circular dichroism
Protein Sci., July 1, 2003; 12(7): 1507 - 1521.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Dvoretsky, E. M. Abusamhadneh, J. W. Howarth, and P. R. Rosevear
Solution Structure of Calcium-saturated Cardiac Troponin C Bound to Cardiac Troponin I
J. Biol. Chem., October 4, 2002; 277(41): 38565 - 38570.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. L. Papish, L. W. Tari, and H. J. Vogel
Dynamic Light Scattering Study of Calmodulin-Target Peptide Complexes
Biophys. J., September 1, 2002; 83(3): 1455 - 1464.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.