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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions.

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.[1]

References

  1. The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. Kowalinski, E., Bange, G., Bradatsch, B., Hurt, E., Wild, K., Sinning, I. FEBS Lett. (2007) [Pubmed]
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