2BBU

solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor

2BBU の概要

• エントリーDOI: 10.2210/pdb2bbu/pdb
• NMR情報: BMRB: 6580
• 分子名称: Suppressor of cytokine signaling 3, GP130 PHOSPHOPEPTIDE (2 entities in total)
• 機能のキーワード: sh2 domain, extended sh2 subdomain, pest motif, protein complex, phosphopeptide, cytokine regulator
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19566.81

構造登録者

Babon, J.J.,Yao, S.,Norton, R.S. (登録日: 2005-10-17, 公開日: 2006-05-02, 最終更新日: 2024-10-16)

主引用文献

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

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: 16630890
DOI: 10.1016/j.molcel.2006.03.024

実験手法

SOLUTION NMR