Figure 1 - Schematic representation of filamin's molecular interactions.

The ABD at the N terminus of filamin contains two calponin homology domains depicted as CHD1 and CHD2. The 24 repeats that follow the ABD most probably fold into antiparallel -sheets and function as interfaces for protein–protein interactions. These repeats not only mediate the dimerization of filamin through the C terminus repeat 24, but also allow filamin to interact with over 30 proteins with great functional diversity. The figure presents a collection of proteins that have been described to interact with filamin directly. The approximate segments involved in each interaction on the filamin protein are depicted as well. In addition to what is presented in the figure, a number of proteins have also been found to bind filamin, although interaction domains on filamin have not been defined. These additional filamin interactors include the glycoprotein Ib–IX complex, the insulin receptor, - and -sarcoglycans, tissue factor, presenilin 1, Trio and Tc-mip.