Yuki Ueda, Shuhei Ohwada, Yoshito Abe, Toshio Shibata, Manabu Iijima, Yukiko Yoshimitsu, Takumi Koshiba, Munehiro Nakata, Tadashi Ueda, Shun-ichiro Kawabata
In the horseshoe crab, the recognition of beta-1,3-D-glucans by factor G triggers hemolymph coagulation. Factor G contains a domain of two tandem xylanase Z-like modules (Z1-Z2), each of which recognizes beta-1,3-D-glucans. To gain an insight into the recognition of beta-1,3-D-glucans from a structural view point, recombinants of Z1-Z2, the C-terminal module Z2, Z2 with a Cys to Ala substitution (Z2A), and its tandem repeat Z2A-Z2A were characterized. Z2 and Z1-Z2, but not Z2A and Z2A-Z2A, formed insoluble aggregates at higher concentrations more than approximately 30 and 3 microM, respectively...
September 15, 2009: Journal of Immunology