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


     

This Article
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 ZHANG, G.
Right arrow Articles by HURLEY, J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by ZHANG, G.
Right arrow Articles by HURLEY, J. H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 6, Issue 4 903-908, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Characterization and crystallization of a minimal catalytic core domain from mammalian type II adenylyl cyclase

G. ZHANG, Y. LIU, J. QIN, B. VO, W. J. TANG, A. E. RUOHO and J. H. HURLEY
Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580

Adenylyl cyclases play a pivotal role in signal transduction by carrying out the regulated synthesis of cyclic AMP. The nine cloned mammalian adenylyl cyclases all share two conserved regions of sequence, C(1) and C(2), which are homologous to each other and are together responsible for catalytic activity. Recombinant C(1) and C(2) domains catalyze the synthesis of cyclic AMP when they are mixed and activated by forskolin, and C(2) domains alone also manifest reduced levels of forskolin-stimulated enzyme activity. Using limited proteolysis and mass spectrometry, we have mapped the boundaries of a minimal stable and active C(2) catalytic domain to residues 871-1090 of type II adenylyl cyclase. We report the properties and crystallization of this trimmed domain, termed IIC(2)-{Delta}4. Crystals belong to space group P4(n)2(1)2, where n = 1 or 3; a = b = 81.3, and c = 180.5 A; and there are two molecules per asymmetric unit related by an approximate body centering operation. Flash-frozen crystals diffract anisotropically to 2.2 A along the c* direction and to 2.8 A along the a* and b* directions using synchrotron radiation.
Add to CiteULike CiteULike   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
 Pharmacol. Rev.Home page
N. Dzimiri
Regulation of beta -Adrenoceptor Signaling in Cardiac Function and Disease
Pharmacol. Rev., September 1, 1999; 51(3): 465 - 502.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. H. Hurley
Structure, Mechanism, and Regulation of Mammalian Adenylyl Cyclase
J. Biol. Chem., March 19, 1999; 274(12): 7599 - 7602.
[Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
W.-J. Tang and J. H. Hurley
Catalytic Mechanism and Regulation of Mammalian Adenylyl Cyclases
Mol. Pharmacol., August 1, 1998; 54(2): 231 - 240.
[Full Text]

Home page
 ScienceHome page
J. J. Tesmer, R. K. Sunahara, A. G. Gilman, and S. R. Sprang
Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with Gsalpha ·GTPgamma S
Science, December 12, 1997; 278(5345): 1907 - 1916.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Liu, A. E. Ruoho, V. D. Rao, and J. H. Hurley
Catalytic mechanism of the adenylyl and guanylyl cyclases: Modeling and mutational analysis
PNAS, December 9, 1997; 94(25): 13414 - 13419.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Protein Society.