Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (7)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Sheffield, P. J.
Right arrow Articles by Derewenda, Z. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sheffield, P. J.
Right arrow Articles by Derewenda, Z. S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 14, No. 7, 513-519, July 2001
© 2001 Oxford University Press

Preparation and crystal structure of the recombinant {alpha}1/{alpha}2 catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib

Peter J. Sheffield,1, Todd W.P. McMullen, Jia Li, Yew-Seng Ho, Sarah M. Garrard, Urszula Derewenda and Zygmunt S. Derewenda,2

Department of Molecular Physiology and Biological Physics, University of Virginia, Health Sciences Center, Charlottesville, VA 22906–0011, USA

The intracellular form of mammalian platelet activating factor acetylhydrolase found in brain (PAF-AH Ib) is thought to play a critical role in control in neuronal migration during cortex development. This oligomeric complex consists of a homodimer of the 45 kDa (ß) LIS1 protein, the product of the causative gene for type I lissencephaly, and, depending on the developmental stage and species, one of three possible pairs of two homologous ~26 kDa {alpha}-subunits, which harbor all of the catalytic activity. The exact composition of this complex depends on the expression patterns of the {alpha}1 and {alpha}2 genes, exhibiting tissue specificity and developmental control. All three possible dimers ({alpha}1/{alpha}1, {alpha}1/{alpha}2 and {alpha}2/{alpha}2) were identified in tissues. The {alpha}1/{alpha}2 heterodimer is thought to play an important role in fetal brain. The structure of the {alpha}1/{alpha}1 homodimer was solved earlier in our laboratory at 1.7 Å. We report here the preparation of recombinant {alpha}1/{alpha}2 heterodimers using a specially constructed bi-cistronic expression vector. The approach may be useful in studies of other systems where pure heterodimers of recombinant proteins are required. The {alpha}1/{alpha}2 dimer has been crystallized and its structure was solved at 2.1 Å resolution by molecular replacement. These results set the stage for a detailed characterization of the PAF-AH Ib complex.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
T. M. Bjerkan, C. L. Bender, H. Ertesvag, F. Drablos, M. K. Fakhr, L. A. Preston, G. Skjak-Braek, and S. Valla
The Pseudomonas syringae Genome Encodes a Combined Mannuronan C-5-epimerase and O-Acetylhydrolase, Which Strongly Enhances the Predicted Gel-forming Properties of Alginates
J. Biol. Chem., July 9, 2004; 279(28): 28920 - 28929.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Liu, C. Jin, and C. Jin
CMP-N-Acetylneuraminic Acid Synthetase from Escherichia coli K1 Is a Bifunctional Enzyme: IDENTIFICATION OF MINIMAL CATALYTIC DOMAIN FOR SYNTHETASE ACTIVITY AND NOVEL FUNCTIONAL DOMAIN FOR PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE ACTIVITY
J. Biol. Chem., April 23, 2004; 279(17): 17738 - 17749.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.