Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain.

ABSTRACT: Ubiquitin-interacting motifs (UIMs) are an important class of protein domains that interact with ubiquitin or ubiquitin-like proteins. These approximately 20-residue-long domains are found in a variety of ubiquitin receptor proteins and serve as recognition modules towards intracellular targets, which may be individual ubiquitin subunits or polyubiquitin chains attached to a variety of proteins. Previous structural studies of interactions between UIMs and ubiquitin have shown that UIMs adopt an extended structure of a single alpha-helix, containing a hydrophobic surface with a conserved sequence pattern that interacts with key hydrophobic residues on ubiquitin. In light of this large body of structural studies, details regarding the presence and the roles of structural dynamics and plastic

SUBMITTER: Sgourakis NG 

PROVIDER: S-EPMC2854419 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature