JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Wolfgang, C. L.
Right arrow Articles by Soprano, D. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wolfgang, C. L.
Right arrow Articles by Soprano, D. R.
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?

Volume 272, Number 2, Issue of January 10, 1997 pp. 746-753
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification of Sulfhydryl-modified Cysteine Residues in the Ligand Binding Pocket of Retinoic Acid Receptor beta

(Received for publication, July 9, 1996, and in revised form, September 25, 1996)

Christopher L. Wolfgang Dagger , Zhen-ping Zhang Dagger , Jerome L. Gabriel Dagger , Ronald A. Pieringer Dagger , Kenneth J. Soprano par and Dianne Robert Soprano Dagger

From the Dagger  Department of Biochemistry,  Fels Institute for Cancer Research and Molecular Biology and par  Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140

The diverse biological functions of retinoic acid (RA) are mediated through retinoic acid receptors (RARs) and retinoid X receptors. RARs contain a high affinity binding site for RA which is sensitive to treatment with sulfhydryl modification reagents. In an attempt to identify which Cys residues are important for this loss of binding, we created three site-specific RARbeta mutants: C228A, C258A, and C267A. The affinity for RA of all three mutant receptors was in the range of that of the wild type protein, suggesting that none of these Cys residues are critical for RA binding. Rather, these modified Cys residue(s) function to sterically hinder RA binding; however, the modified Cys residues critical for the inhibition of binding differ depending on the reagent employed. Only modification of Cys228 is necessary to inhibit RA binding when RARbeta is modified by reagents which transfer large bulky groups while both Cys228 and Cys267 must be modified when a small functional group is transferred. These data suggest that both Cys228 and Cys267 but not Cys258 lie in the ligand binding pocket of RARbeta . However, Cys228 lies closer to the opening of the RARbeta ligand binding pocket whereas Cys267 lies more deeply buried.


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
 GlycobiologyHome page
K. Kumari and P. H. Weigel
Identification of a membrane-localized cysteine cluster near the substrate-binding sites of the Streptococcus equisimilis hyaluronan synthase
Glycobiology, May 1, 2005; 15(5): 529 - 539.
[Abstract] [Full Text] [PDF]

Home page
 J AndrolHome page
F. Richter, A. Joyce, F. Fromowitz, S. Wang, J. Watson, R. Watson, R. J. Irwin Jr, and H. F. S. Huang
Immunohistochemical Localization of the Retinoic Acid Receptors in Human Prostate
J Androl, November 1, 2002; 23(6): 830 - 838.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Kumari, V. L. Tlapak-Simmons, B. A. Baggenstoss, and P. H. Weigel
The Streptococcal Hyaluronan Synthases Are Inhibited by Sulfhydryl-modifying Reagents, but Conserved Cysteine Residues Are Not Essential for Enzyme Function
J. Biol. Chem., April 12, 2002; 277(16): 13943 - 13951.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z.-P. Zhang, C. J. Gambone, J. L. Gabriel, C. L. Wolfgang, K. J. Soprano, and D. R. Soprano
Arg278, but Not Lys229 or Lys236, Plays an Important Role in the Binding of Retinoic Acid by Retinoic Acid Receptor gamma
J. Biol. Chem., December 18, 1998; 273(51): 34016 - 34021.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
C. D. Katsetos, I. Stadnicka, J. C. Boyd, H. Ehya, S. Zheng, C. M. Soprano, H. S. Cooper, A. S. Patchefsky, D. R. Soprano, and K. J. Soprano
Cellular Distribution of Retinoic Acid Receptor-{alpha} Protein in Serous Adenocarcinomas of Ovarian, Tubal, and Peritoneal Origin : Comparison with Estrogen Receptor Status
Am. J. Pathol., August 1, 1998; 153(2): 469 - 480.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Scafonas, C. L. Wolfgang, J. L. Gabriel, K. J. Soprano, and D. R. Soprano
Differential Role of Homologous Positively Charged Amino Acid Residues for Ligand Binding in Retinoic Acid Receptor alpha Compared with Retinoic Acid Receptor beta
J. Biol. Chem., April 25, 1997; 272(17): 11244 - 11249.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.