2BBU
solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor
Summary for 2BBU
| Entry DOI | 10.2210/pdb2bbu/pdb |
| NMR Information | BMRB: 6580 |
| Descriptor | Suppressor of cytokine signaling 3, GP130 PHOSPHOPEPTIDE (2 entities in total) |
| Functional Keywords | sh2 domain, extended sh2 subdomain, pest motif, protein complex, phosphopeptide, cytokine regulator |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 19566.81 |
| Authors | Babon, J.J.,Yao, S.,Norton, R.S. (deposition date: 2005-10-17, release date: 2006-05-02, Last modification date: 2024-10-16) |
| Primary citation | Babon, J.J.,McManus, E.J.,Yao, S.,DeSouza, D.P.,Mielke, L.A.,Sprigg, N.S.,Willson, T.A.,Hilton, D.J.,Nicola, N.A.,Baca, M.,Nicholson, S.E.,Norton, R.S. The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability Mol.Cell, 22:205-216, 2006 Cited by PubMed Abstract: SOCS3 is essential for regulating the extent, duration, and specificity of cellular responses to cytokines such as G-CSF and IL-6. Here we describe the solution structure of SOCS3, the first structure determined for any SOCS protein, in complex with a phosphotyrosine-containing peptide from the IL-6 receptor signaling subunit gp130. The structure of the complex shows that seven peptide residues form a predominantly hydrophobic binding motif. Regions outside the SOCS3 SH2 domain are important for ligand binding, in particular, a single 15 residue alpha helix immediately N-terminal to the SH2 domain makes direct contacts with the phosphotyrosine binding loop and, in part, determines its geometry. The SH2 domain itself is remarkable in that it contains a 35 residue unstructured PEST motif insertion that is not required for STAT inhibition. The PEST motif increases SOCS3 turnover and affects its degradation pathway, implying that it has an important regulatory role inside the cell. PubMed: 16630890DOI: 10.1016/j.molcel.2006.03.024 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
