1XR0
Structural Basis of SNT PTB Domain Interactions with Distinct Neurotrophic Receptors
Summary for 1XR0
| Entry DOI | 10.2210/pdb1xr0/pdb |
| Descriptor | Basic fibroblast growth factor receptor 1, FGFR signalling adaptor SNT-1 (2 entities in total) |
| Functional Keywords | fgfr, snt, phosphotyrosine binding domain, ptb, trk, npxpy motif, signaling protein-growth factor receptor complex, signaling protein/growth factor receptor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Membrane; Single-pass type I membrane protein: P11362 Endomembrane system: Q8WU20 |
| Total number of polymer chains | 2 |
| Total formula weight | 17498.77 |
| Authors | Dhalluin, C.,Yan, K.S.,Plotnikova, O.,Lee, K.W.,Zeng, L.,Kuti, M.,Mujtaba, S.,Goldfarb, M.P.,Zhou, M.-M. (deposition date: 2004-10-13, release date: 2004-11-02, Last modification date: 2024-05-22) |
| Primary citation | Dhalluin, C.,Yan, K.S.,Plotnikova, O.,Lee, K.W.,Zeng, L.,Kuti, M.,Mujtaba, S.,Goldfarb, M.P.,Zhou, M.-M. Structural Basis of SNT PTB Domain Interactions with Distinct Neurotrophic Receptors Mol.Cell, 6:921-929, 2000 Cited by PubMed Abstract: SNT adaptor proteins transduce activation of fibroblast growth factor receptors (FGFRs) and neurotrophin receptors (TRKs) to common signaling targets. The SNT-1 phosphotyrosine binding (PTB) domain recognizes activated TRKs at a canonical NPXpY motif and, atypically, binds to nonphosphorylated FGFRs in a region lacking tyrosine or asparagine. Here, using NMR and mutational analyses, we show that the PTB domain utilizes distinct sets of amino acid residues to interact with FGFRs or TRKs in a mutually exclusive manner. The FGFR1 peptide wraps around the beta sandwich structure of the PTB domain, and its binding is possibly regulated by conformational change of a unique C-terminal beta strand in the protein. Our results suggest mechanisms by which SNTs serve as molecular switches to mediate the essential interplay between FGFR and TRK signaling during neuronal differentiation. PubMed: 11090629DOI: 10.1016/S1097-2765(05)00087-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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