NMR Characterisation Of A Novel Cell Surface Receptor

and Bridget C.Mabbutt^*

^*Initiative in Biomolecular Structure (IBiS), School of Biochemistry and Molecular Genetics, University of New South Wales, NSW 2052 and ⁺Macquarie University Centre for Analytical Biotechnology (MUCAB), School of Biological Sciences, Macquarie University, NSW 2109

During the processes of differentiation and development, cells recognise each other and adhere. Cell surface glycoproteins mediate the intercellular interactions involved in these key biological processes. The glycoprotein prespore-specific antigen (PsA), a classic cell surface marker for spore formation in Dictyostelium discoideum at slug phase, is thought to participating in the process of cell-cell adhesion via heterophilic binding interactions.

We describe results of NMR studies of the three-dimensional organisation and structure of PsA, and provide evidence that this protein comprises a new type of cell surface protein fold.