Fig. 1: FXII deletion mutants.
From: Identification of the factor XII contact activation site enables sensitive coagulation diagnostics
A Schematic structure of the zymogen forms of human full-length FXII (FXII_fl) and FXII deletion mutants lacking various domains or fragments. The N-terminal grey square represents the 19 amino acid-long signal peptide. The heavy chain of mature FXII consists of six domains: the fibronectin type-II (Fib-II, red), the first epidermal growth factor like (EGF-I, green), the fibronectin type-I (Fib-I, orange), the second EGF-like (EGF-II, violet), the Kringle (KR, yellow), and the proline-rich (PR, blue) domains. The C-terminal light chain (LC) contains the catalytic triad of a serine protease and is marked in grey. PR-I, PR-II and PR-III represent the N-terminal, central and C-terminal fragment of the PR domain, respectively. FXII_ΔEGF-II-1 and FXII_ΔEGFII-2 are mutants deficient in the N- and C-terminal portions of the EGF-I domain, respectively. Numbers on top indicate amino acid residues of the mature FXII protein. B, C HEK293 cells were transiently transfected with vectors coding for FXII mutants shown in panel A. After 48 h of transfection, washed HEK293 cells (B) or cell supernatants (C) were analysed for FXII protein using SDS PAGE under reducing conditions and western blotting with polyclonal anti-FXII antibodies. Representative images of n = 5 individual experiments. In the bottom panel, + or – indicate whether mutants were secreted into the cell supernatant. Mw: molecular weight, kDa: kilodalton.
