Homodimer Folding and Binding
The formation of an interface through the association of two identical monomers (homodimers) is common in cellular regulation. A number of structures have been known till date in homodimer complex form. The folding mechanism is also known for some of these homodimers. They fold through two-state (2S) without the formation of an intermediate or through three-state (3S) with the formation of an intermediate. The 3S proteins either form a monomer intermediate (3SMI) or a dimer intermediate (3SDI) in establishing a biologically active interface. Therefore, it is of interest to create relationship between structural features and folding mechanism. Estimating the relationship between known homodimer structures with known folding data is challenging. The structural differences among 2S, 3SMI, and 3SDI are discussed using 3D homodimer structures.