Premium
The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions
Author(s) -
Kowalinski Eva,
Bange Gert,
Bradatsch Bettina,
Hurt Ed,
Wild Klemens,
Sinning Irmgard
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.024
Subject(s) - methionine , aminopeptidase , biochemistry , binding site , enzyme , chemistry , plasma protein binding , transcription factor , transcription (linguistics) , microbiology and biotechnology , biology , leucine , amino acid , gene , linguistics , philosophy
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 Å 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.