JBC INTERFERin siRNA transfection reagent

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


     

A more recent version of this article appeared on March 21, 2003
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
278/13/11320    most recent
M211820200v1
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 Rose, T.
Right arrow Articles by Di Cera, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rose, T.
Right arrow Articles by Di Cera, E.
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 December 18, 2002
J. Biol. Chem, 10.1074/jbc.M211820200
Submitted on November 20, 2002
Revised on December 18, 2002
Accepted on December 18, 2002

Three-dimensional models of proteases involved in patterning of the Drosophila embryo: Crucial role of predicted cation binding sites

Thierry Rose, Ellen K. LeMosy, Angelene M. Cantwell, Dolly Banerjee-Roy, James B. Skeath, and Enrico Di Cera

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO 63110

Corresponding Author: enrico{at}biochem.wustl.edu

Three-dimensional models of the catalytic domains of Nudel (Ndl), Gastrulation Defective (Gd), Snake (Snk) and Easter (Ea) and their complexes with substrate suggest a possible organization of the enzyme cascade controlling the dorso-ventral fate of the fruit fly embryo. The models predict that Gd activates Snk, which in turn activates Ea. Gd can be activated either autoproteolytically or by Ndl. 3D-models of each enzyme-substrate complex in the cascade rationalize existing mutagenesis data and the associated phenotypes. The models also predict unanticipated features like a Ca2+ binding site in Ea and a Na+ binding site in Ndl and Gd. These binding sites likely play a crucial role in vivo as suggested by mutant enzymes introduced into embryos as mRNAs. Mutations in Gd that eliminate Na+ binding cause an apparent increase in activity, whereas mutations in Ea that abrogate Ca2+ binding result in the complete loss of activity. A mutation in Ea predicted to introduce Na+ binding results in apparently increased activity with ventralization of the embryo, an effect not observed with wild-type Ea mRNA.


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
A. N. R. Weber, M. Gangloff, M. C. Moncrieffe, Y. Hyvert, J.-L. Imler, and N. J. Gay
Role of the Spatzle Pro-domain in the Generation of an Active Toll Receptor Ligand
J. Biol. Chem., May 4, 2007; 282(18): 13522 - 13531.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Piao, S. Kim, J. H. Kim, J. W. Park, B. L. Lee, and N.-C. Ha
Crystal Structure of the Serine Protease Domain of Prophenoloxidase Activating Factor-I
J. Biol. Chem., April 6, 2007; 282(14): 10783 - 10791.
[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.