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Blood, Vol. 94 No. 11 (December 1), 1999: pp. 3947-3950

Characterization of the Murine Platelet &b.alpha;IIb Gene and Encoded cDNA

Michael A. Thornton and Mortimer Poncz

From the Department of Pediatrics, University of Pennsylvania School of Medicine, Philadelphia, PA.

The alpha IIb/beta 3 receptor is central to platelet aggregation. Biological studies of this receptor have been limited by the inability to reproduce alpha IIb/beta 3 function in a cell system. Increasingly, efforts are being directed at studies of this receptor in mice models. The structure of murine (m) beta 3 has been reported. We now have sequenced the malpha IIb gene and found that it has the same size and organization as the human gene. The exon/intron borders are reported here, as are the distances between exons. malpha IIb protein is 1,033 amino acids (aa), 7 and 5 aa shorter than human (h) and rodent (r) alpha IIb, respectively, with 79% and 90% homology, respectively. As part of the comparative analysis of the 3 known alpha IIb chains included in this report, we found that a particular region of the alpha IIb N-terminal beta -propeller is highly conserved and speculate that it directly participates in ligand binding.


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