Structural studies offer a framework for understanding the role of properdin in the alternative pathway and beyond.

ABSTRACT: Structures of alternative pathway proteins have offered a comprehensive structural basis for understanding the molecular mechanisms governing activation and regulation of the amplification pathway of the complement cascade. Although properdin (FP) is required in vivo to sustain a functional alternative pathway, structural studies have been lagging behind due to the extended structure and polydisperse nature of FP. We review recent progress with respect to structure determination of FP and its proconvertase/convertase complexes. These structures identify in detail regions in C3b, factor B and FP involved in their mutual interactions. Structures of FP oligomers obtained by integrative studies have shed light on how FP activity depends on its oligomerization state. The accumulated structural

SUBMITTER: Pedersen DV 

PROVIDER: S-EPMC10087229 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature