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Characterization of the murine platelet alphaIIb gene and encoded cDNA.
The alphaIIb/beta3 receptor is central to platelet aggregation. Biological studies of this receptor have been limited by the inability to reproduce alphaIIb/beta3 function in a cell system. Increasingly, efforts are being directed at studies of this receptor in mice models. The structure of murine (m) beta3 has been reported. We now have sequenced the malphaIIb 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. malphaIIb protein is 1,033 amino acids (aa), 7 and 5 aa shorter than human (h) and rodent (r) alphaIIb, respectively, with 79% and 90% homology, respectively. As part of the comparative analysis of the 3 known alphaIIb chains included in this report, we found that a particular region of the alphaIIb N-terminal beta-propeller is highly conserved and speculate that it directly participates in ligand binding.
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