Ontology highlight
ABSTRACT:
SUBMITTER: Haririnia A
PROVIDER: S-EPMC2254529 | biostudies-literature | 2008 Jan
REPOSITORIES: biostudies-literature
Haririnia Aydin A Verma Rati R Purohit Nisha N Twarog Michael Z MZ Deshaies Raymond J RJ Bolon Dan D Fushman David D
Journal of molecular biology 20071113 4
Ubiquitin (Ub) is one of the most highly conserved signaling proteins in eukaryotes. In carrying out its myriad functions, Ub conjugated to substrate proteins interacts with dozens of receptor proteins that link the Ub signal to various biological outcomes. Here we report mutations in conserved residues of Ub's hydrophobic core that have surprisingly potent and specific effects on molecular recognition. Mutant Ubs bind tightly to the Ub-associated domain of the receptor proteins Rad23 and hHR23A ...[more]