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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.


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