CEXS-UPF: A study reveals a hitherto unknown protein affinity

CEXS-UPF: A study reveals a hitherto unknown protein affinity

News from CEXS-UPF

For many years it was thought that proteins had to fold into structured scaffolds in order to have any meaningful function. This view has been upended in the last decade, as it has become clear that there are many important regions of proteins that have no permanent structure. These proteins are commonly called intrinsically disordered proteins, or IDPs.

IDPs remain largely unstructured under native conditions, resembling random-coil polymers akin to the unfolded states of proteins. Phosphorylation plays a key role in many signal transduction processes, and preferentially targets intrinsically disordered protein domains. Present in more than 50% of eukaryotic proteins, IDPs perform a plethora of biological functions and are commonly associated with a variety of human diseases, particularly cancer.

Cells have many ways to modify IDPs and their interactions, but the specific mechanisms are not yet fully understood. In work coordinated by Gianni De Fabritiis researcher ICREA at CEXS Department and head of the l aboratory of Computational Biophysics at GRIB (IMIM - UPF), published in Nature Communications on October 28th. "we show that a modification to a disordered protein known as the Kinase Inducible Domain (KID) not only modulates what shapes it takes, but importantly the time it takes for the changes to happen", said De Fabritiis.

More information:

Nathaliel Stanley, Santiago Esteban-Martín i Gianni De Fabritiis (2014), "Kinetic modulation of a disordered protein domain by phosphorylation", Nature Communication, 28th October