8Z0N
Structure and dynamics of Drk-SH2 domain and its site-specific interaction with Sev
Summary for 8Z0N
| Entry DOI | 10.2210/pdb8z0n/pdb |
| Related | 7Y4N |
| Descriptor | Growth factor receptor-bound protein 2 (1 entity in total) |
| Functional Keywords | src homology 2, drosophila, downstream receptor kinase, sev, growth factor receptor-bound protein 2, peptide binding protein, solution structure, dynamics |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 10739.17 |
| Authors | Sayeesh, P.M.,Mayumi, I.,Inomata, K.,IKeya, T.,Ito, Y. (deposition date: 2024-04-10, release date: 2025-03-19) |
| Primary citation | Sayeesh, P.M.,Iguchi, M.,Inomata, K.,Ikeya, T.,Ito, Y. Structure and Dynamics of Drk-SH2 Domain and Its Site-Specific Interaction with Sev Receptor Tyrosine Kinase. Int J Mol Sci, 25:-, 2024 Cited by PubMed Abstract: The downstream receptor kinase (Drk), a homologue of human GRB2, participates in the signal transduction from the extracellular to the intracellular environment. Drk receives signals through the interaction of its Src homology 2 (SH2) domain with the phosphorylated tyrosine residue in the receptor tyrosine kinases (RTKs). Here, we present the solution NMR structure of the SH2 domain of Drk (Drk-SH2), which was determined in the presence of a phosphotyrosine (pY)-containing peptide derived from a receptor tyrosine kinase, Sevenless (Sev). The solution structure of Drk-SH2 possess a common SH2 domain architecture, consisting of three β strands imposed between two α helices. Additionally, we interpret the site-specific interactions of the Drk-SH2 domain with the pY-containing peptide through NMR titration experiments. The dynamics of Drk-SH2 were also analysed through NMR-relaxation experiments as well as the molecular dynamic simulation. The docking simulations of the pY-containing peptide onto the protein surface of Drk-SH2 provided the orientation of the peptide, which showed a good agreement with the analysis of the SH2 domain of GRB2. PubMed: 38928093DOI: 10.3390/ijms25126386 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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