Human antigen R (HuR) is a ubiquitous 32 kDa protein comprising three RNA 
Recognition Motifs (RRMs), whose main function is to bind Adenylate and 
uridylate Rich Elements (AREs) in 3' UnTranslated Regions (UTRs) of mRNAs. In 
addition to binding RNA molecules, the third domain (RRM3) is involved in HuR 
oligomerization and apoptotic signaling. The RRM3 monomer is able to dimerize, 
with its self-binding affinity being dependent on ionic strength. Here we 
provide a deeper structural insight into the nature of the encounter complexes 
leading to the formation of RRM3 dimers by using Brownian Dynamics and Molecular 
Dynamics. Our computational data show that the initial unspecific encounter 
follows a downhill pathway until reaching an optimum conformation stabilized by 
hydrophobic interactions.