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FEBS Lett. 2007 Sep 18;581(23):4450-4. Epub 2007 Aug 27.

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

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1
Heidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.

Abstract

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.

PMID:
17765895
DOI:
10.1016/j.febslet.2007.08.024
[Indexed for MEDLINE]
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