The F-MuLV receptor-binding domain forms part of the retroviral envelope glycoprotein in the murine leukaemia virus. Envelope glycoproteins are synthesized as single chain precursors, which are subsequently cleaved into the surface subunit (SU) and the transmembrane subunit TM. The N-terminal half of SU forms the receptor-binding domain (RBD), which is responsible for binding to the cell surface receptor, the cationic amino acid transporter mCAT-1. The RBD is structurally partitioned into a conserved beta sandwich framework of Greek key topology and a variable helical loop subdomain. The RBD contains three variable regions, VRA, VRB and VRC, which vary in sequence and length between MuLVs that use different receptors. VRA and VRB are closely associated with one another in the helical subdomain. There is a putative receptor-binding pocket in VRA, which may play a role in helping to determine receptor specificity.