The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions
Authors: Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I
CellNetworks People: Hurt Ed, Sinning Irmgard
Journal: FEBS Lett. 2007 Sep 18;581(23):4450-4

The ErbB-3 receptor binding protein (Ebp1) is a member of the proliferation-associated 2G4 (PA2G4) family implicated in regulation of cell growth and differentiation. Here, we report the crystal structure of the human Ebp1 at 1.6 A resolution. The protein has the conserved pita bread fold of methionine aminopeptidases, but without the characteristic enzymatic activity. Moreover, Ebp1 is known to interact with a number of proteins and RNAs involved in either transcription regulation or translation control. The structure provides insights in how Ebp1 discriminates between its different interaction partners.