1DDM
SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE
Summary for 1DDM
| Entry DOI | 10.2210/pdb1ddm/pdb |
| Related | 2NMB |
| Descriptor | NUMB PROTEIN, NUMB ASSOCIATE KINASE (2 entities in total) |
| Functional Keywords | complex, signal transduction, phosphotyrosine binding domain (ptb), asymmetric cell division, signaling protein-transferase complex, signaling protein/transferase |
| Biological source | Drosophila melanogaster (fruit fly) More |
| Cellular location | Nucleus: P16554 |
| Total number of polymer chains | 2 |
| Total formula weight | 16554.78 |
| Authors | Zwahlen, C.,Li, S.C.,Kay, L.E.,Pawson, T.,Forman-Kay, J.D. (deposition date: 1999-11-11, release date: 2000-04-10, Last modification date: 2024-05-22) |
| Primary citation | Zwahlen, C.,Li, S.C.,Kay, L.E.,Pawson, T.,Forman-Kay, J.D. Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb. EMBO J., 19:1505-1515, 2000 Cited by PubMed Abstract: The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb is involved in the formation of multiple protein complexes in vivo and can bind a diverse array of peptide sequences in vitro. To investigate the structural basis for the promiscuous nature of this protein module, we have determined its solution structure by NMR in a complex with a peptide containing an NMSF sequence derived from the Numb-associated kinase (Nak). The Nak peptide was found to adopt a significantly different structure from that of a GPpY sequence-containing peptide previously determined. In contrast to the helical turn adopted by the GPpY peptide, the Nak peptide forms a beta-turn at the NMSF site followed by another turn near the C-terminus. The Numb PTB domain appears to recognize peptides that differ in both primary and secondary structures by engaging various amounts of the binding surface of the protein. Our results suggest a mechanism through which a single PTB domain might interact with multiple distinct target proteins to control a complex biological process such as asymmetric cell division. PubMed: 10747019DOI: 10.1093/emboj/19.7.1505 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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