Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Maliszewski, C.R. et al.

The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization.

CD39, a 70- to 100-kDa molecule expressed primarily on activated lymphoid cells, was previously shown to mediate B cell homotypic adhesion when ligated with a subset of anti-CD39 mAbs. In the present study, we describe the cloning and molecular characterization of human and murine CD39. The nucleotide sequence of human CD39 includes an open reading frame encoding a putative 510 amino acid protein with six potential N-linked glycosylation sites, 11 Cys residues, and two potential transmembrane regions. Murine CD39 shares 75% amino acid sequence identity with human CD39 but fails to cross-react with anti-human CD39 mAbs. Although there were no significant similarities with other mammalian genes, considerable homology was found between CD39 and a guanosine diphosphatase from yeast. A series of mouse-human hybrid molecules was constructed to determine the general topology of CD39 and the location of a biologically functional epitope. These findings and supporting evidence from an anti-CD39 mAb-selected phage peptide display library indicate a likely model wherein a short intracellular N-terminus is followed by a large extracellular loop containing the epitope recognized by stimulatory anti-CD39 mAbs, and a short intracellular C terminus. The results demonstrate that CD39 is a novel cell surface glycoprotein with unusual structural characteristics.[1]

References

The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. Maliszewski, C.R., Delespesse, G.J., Schoenborn, M.A., Armitage, R.J., Fanslow, W.C., Nakajima, T., Baker, E., Sutherland, G.R., Poindexter, K., Birks, C. J. Immunol. (1994) [Pubmed]

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