| First Author | Qiu C | Year | 2008 |
| Journal | J Biol Chem | Volume | 283 |
| Issue | 5 | Pages | 2734-40 |
| PubMed ID | 18045866 | Mgi Jnum | J:131332 |
| Mgi Id | MGI:3773504 | Doi | 10.1074/jbc.M703523200 |
| Citation | Qiu C, et al. (2008) Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site. J Biol Chem 283(5):2734-40 |
| abstractText | Memo (mediator of ErbB2-driven cell motility) is a 297-amino-acid protein recently shown to co-precipitate with the C terminus of ErbB2 and be required for ErbB2-driven cell motility. Memo is not homologous to any known signaling proteins, and how it mediates ErbB2 signals is not known. To provide a molecular basis for understanding Memo function, we have determined and report here the 2.1A crystal structure of human Memo and show it be homologous to class III nonheme iron-dependent dioxygenases, a structural class that now includes a zinc-binding protein of unknown function. No metal binding or enzymatic activity can be detected for Memo, but Memo does bind directly to a specific ErbB2-derived phosphopeptide encompassing Tyr-1227 using its vestigial enzymatic active site. Memo thus represents a new class of phosphotyrosine-binding protein. |
