Molecular insights into the surface regions of ubiquitin recognized by interacting proteins

Understanding the wide variety of targeting functions imposed by the covalent attachment of ubiquitin requires molecular analyses of its interaction with binding proteins. Evidence is now available that demonstrates the importance of electrostatic and hydrophobic forces (mechanistically weak but functionally important) that provide the framework for covalent bond formation in these interactions. In this report, we introduce available information on the structural features of ubiquitin recognized by various ubiquitin-interacting proteins, including our recent results on the YUH1-Ub system.