Article
Surfactant protein A without the interruption of Gly-X-Y repeats loses a kink of oligomeric structure and exhibits impaired phospholipid liposome aggregation ability.
Biochemistry - 5 Dec 2006
Uemura Tatsuki, Sano Hitomi, Katoh Tsuyoshi, Nishitani Chiaki, Mitsuzawa Hiroaki, Shimizu Takeyuki, Kuroki Yoshio
Abstract excerpt
Pulmonary surfactant protein A (SP-A) belongs to the collectin subgroup of the C-type lectin superfamily. SP-A oligomerizes as an octadecamer, which forms a flower bouquet-like structure. A collagen-like domain of human SP-A consists of 23 Gly-X-Y repeats with an interruption near the midpoint of this domain. This interruption causes a kink, but its role remains unknown. To define the importance of the kink...
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