Advertisement
JBC

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


     

A more recent version of this article appeared on November 2, 2007
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
282/44/32256    most recent
M706231200v1
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Brock, M.
Right arrow Articles by Cheng, X.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brock, M.
Right arrow Articles by Cheng, X.
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 September 4, 2007
J. Biol. Chem, 10.1074/jbc.M706231200
Submitted on July 30, 2007
Revised on September 4, 2007
Accepted on September 4, 2007

Conformational analysis of EPAC activation using amide hydrogen/deuterium exchange mass spectrometry

Melissa Brock, Fenghui Fan, Fang C. Mei, Sheng Li, Christopher Gessner, Virgil L. Woods . Jr, and Xiaodong Cheng

Pharmacology and Toxicology, The University of Texas Medical Branch, Galveston, TX 77555-1031

Corresponding Author: xcheng{at}utmb.edu

Exchange proteins directly activated by cAMP (Epac) play important roles in mediating the effects of cAMP through the activation of down-stream small GTPases, Rap. To delineate the mechanism of Epac activation, we probed the conformation and structural dynamics of Epac using amide hydrogen/deuterium exchange and structural modeling. Our studies show that cAMP induces significant conformational changes that lead to a spatial rearrangement of the regulatory components of Epac and allows the exposure of the catalytic core for effector binding without imposing significant conformational change on the catalytic core. Homology modeling and comparative structural analyses of the cAMP binding domains of Epac and PKA lead to a model of Epac activation, in which Epac and PKA activation by cAMP employs the same underlying principal although the detailed structural and conformational changes associated with Epac and PKA activation are significantly different.


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
 J. Biol. Chem.Home page
R. Das, M. T. Mazhab-Jafari, S. Chowdhury, S. SilDas, R. Selvaratnam, and G. Melacini
Entropy-driven cAMP-dependent Allosteric Control of Inhibitory Interactions in Exchange Proteins Directly Activated by cAMP
J. Biol. Chem., July 11, 2008; 283(28): 19691 - 19703.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. M. Harper, H. Wienk, R. W. Wechselberger, J. L. Bos, R. Boelens, and H. Rehmann
Structural Dynamics in the Activation of Epac
J. Biol. Chem., March 7, 2008; 283(10): 6501 - 6508.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement