Aberrant maturation of mutant perforin underlies the clinical diversity of hemophagocytic lymphohistiocytosis
J. Clin. Invest. Kimberly A. Risma, et al. 116:182 doi:10.1172/JCI26217 [Go to this article.]

Figure 6
Schematic representation of the human perforin protein showing the location of amino acid transitions evaluated in the current study. The horizontal bar represents the perforin protein with its theoretical functional domains: the membrane attack complex domain (MACPRF), the EGF-like domain (EGF), and a domain homologous to the C2 domain of PKC (C2) (27, 42). The areas with gradient shading mark the signal peptide and the C-terminal peptide, which are cleaved during maturation. Class 1: missense mutations with partial maturation of perforin (in b capital letters above bar); class 2: no apparent maturation of perforin (in is above bar); class 3: no recognizable forms of perforin (below the bar). PRF1-N252S (boxed) is a polymorphism.