The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.

ABSTRACT: Anastellin is a small recombinant fragment derived from the extracellular matrix protein fibronectin; it comprises the first type III (FN3) domain without the two N-terminal β-strands. It inhibits angiogenesis, tumor growth, and metastasis in mouse models and requires endogenous fibronectin for its in vivo anti-angiogenic activity. It binds to fibronectin in vitro and converts the soluble protein to insoluble fibrils that structurally and functionally resemble fibronectin fibrils deposited in the extracellular matrix by cells. Anastellin binds to several FN3 domains in fibronectin, but how it interacts with these domains and why the interactions lead to aggregation of fibronectin are not well understood. In this work, we investigated the interaction between anastellin and the third FN3 dom

SUBMITTER: Stine JM 

PROVIDER: S-EPMC5612498 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature