Two classes of of proteins selectively interact with the lipid phosphatidylserine (PS).  Some transmembrane transporters, or �flippases,� recognize PS in one monolayer of a membrane and transport this lipid to opposite surface, with the concomitant consumption of ATP.  Other proteins interact with PS-containing membranes in an interfacial fashion and this binding transmits essential cell signals.  The mechanisms by which these two classes of proteins interact with PS are distinct.  Of the two chiral centers in PS, the PS flippase transports only the 1,2-sn-glycerol isomer of this lipid, while interfacial PS binding proteins, such as protein kinase C or clotting factors V and X, recognize selectively the L-serine stereoisomer.  Modifications to other structural elements of PS result in reduction of binding to both classes of these proteins.  These data indicate that two distinct binding site structures have evolved in proteins for the selective recognition of PS in biological membranes.

Substrate specificity of phosphatidylserine transport and binding proteins

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.