Expression, purification, and characterization of a human complement component C3 analog that lacks the C-terminal C345c domain.

ABSTRACT: The complement system consists of a series of soluble and cell-surface proteins that serve numerous roles in innate immunity, development, and homeostasis. Despite its many functions, the central event in the complement system is the proteolytic activation of the 185 kDa complement component 3 (C3) into its opsonin and anaphylatoxin fragments known as C3b (175 kDa) and C3a (10 kDa), respectively. The C3 protein is comprised of thirteen separate structural domains, several of which undergo extensive structural rearrangement upon activation to C3b. In addition to this, the C-terminal C345c domain found in C3, C3b, and the terminal degradation product, C3c (135 kDa), appears to adopt multiple conformations relative to the remainder of the molecule. To facilitate various structure/function stu

SUBMITTER: Ramyar KX 

PROVIDER: S-EPMC6707835 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature