Most proteins interact with only one or a few ligands, but light chain 8 (LC8) is an example of a protein that has more than a hundred binding partners, ranging from viral proteins and motor proteins through to the proteins involved in cell division.
At the Department of Biochemistry and Biophysics at Oregon State University, Professor Elisar Barbar and colleagues have been studying the structure, assembly and regulation of the LC8 protein interaction network and how these interactions affect numerous essential cellular functions.
In a recent interview, Barbar commented that one feature LC-8 binding proteins share is that they are all intrinsically disordered. Disorder is an essential aspect of how intrinsically disordered proteins (IDPs) function. Lacking a stable tertiary structure, these proteins do not fold into a tightly packed native state that presents only one or a few active binding sites. Instead, they sample numerous inter-converting conformations with varying degrees of disorder, some of which can also bind to several folded proteins.