2Q8K
The crystal structure of Ebp1
Summary for 2Q8K
| Entry DOI | 10.2210/pdb2q8k/pdb |
| Descriptor | Proliferation-associated protein 2G4, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ebp1, pa2g4, methionine aminopeptidase, pita-bread, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9UQ80 |
| Total number of polymer chains | 1 |
| Total formula weight | 45402.31 |
| Authors | Kowalinski, E.,Bange, G.,Wild, K.,Sinning, I. (deposition date: 2007-06-11, release date: 2007-09-25, Last modification date: 2023-08-30) |
| Primary citation | Kowalinski, E.,Bange, G.,Bradatsch, B.,Hurt, E.,Wild, K.,Sinning, I. The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. Febs Lett., 581:4450-4454, 2007 Cited by PubMed 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. PubMed: 17765895DOI: 10.1016/j.febslet.2007.08.024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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