Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer.

ABSTRACT: Fibronectin (FN) matrix is crucial for cell and tissue functions during embryonic development, wound healing, and oncogenesis. Assembly of FN matrix fibrils requires FN domains that mediate interactions with integrin receptors and with other FN molecules. In addition, regulation of FN matrix assembly depends on the first two FN type III modules, III(1) and III(2), which harbor FN-binding sites. We propose that interactions between these two modules sequester FN-binding sites in soluble FN and that these sites become exposed by FN conformational changes during assembly. To test the idea that III(1-2) has a compact conformation, we constructed CIIIY, a conformational sensor of III(1-2) based on fluorescent resonance energy transfer between cyan and yellow fluorescent proteins conjugated at i

SUBMITTER: Karuri NW 

PROVIDER: S-EPMC2635030 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature