Fig. 2
From: Immunoregulatory functions and the therapeutic implications of GARP-TGF-β in inflammation and cancer
Structure of the membrane-bound GARP-latent TGF-β1 complex. GARP protein is structurally divided into three domains based on its primary sequence: the extracellular domain, the transmembrane domain, and the intracellular domain. The extracellular domain contains two sets of ten LRRs divided by a proline-rich domain and one C-terminal LRR (LRRCT). Two conserved Cys residues (Cys-192 and Cys-331) are located on the 7th and 12th LRR, respectively, and are responsible for two disulfide bond formation between GARP and Cys-4 of LAP of latent TGF-β