3MBK
The 1.35 A Structure of the Phosphatase Domain of the Suppressor of T Cell Receptor Signalling Protein in Complex with Sulphate
3MBK の概要
| エントリーDOI | 10.2210/pdb3mbk/pdb |
| 関連するPDBエントリー | 2H0Q |
| 分子名称 | Ubiquitin-associated and SH3 domain-containing protein B, SULFATE ION (3 entities in total) |
| 機能のキーワード | pgm, sts-1, signaling protein, low ph, nucleus, phosphoprotein, sh3 domain |
| 由来する生物種 | Mus musculus (mouse) |
| 細胞内の位置 | Cytoplasm : Q8BGG7 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 59582.25 |
| 構造登録者 | |
| 主引用文献 | Jakoncic, J.,Sondgeroth, B.,Carpino, N.,Nassar, N. The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate. Acta Crystallogr.,Sect.F, 66:643-647, 2010 Cited by PubMed Abstract: The suppressor of T-cell signaling (Sts) proteins are multidomain proteins that negatively regulate the signaling of membrane-bound receptors, including the T-cell receptor (TCR) and the epidermal growth-factor receptor (EGFR). They contain at their C-terminus a 2H-phosphatase homology (PGM) domain that is responsible for their protein tyrosine phosphatase activity. Here, the crystal structure of the phosphatase domain of Sts-1, Sts-1(PGM), was determined at pH 4.6. The asymmetric unit contains two independent molecules and each active site is occupied by a sulfate ion. Each sulfate is located at the phosphate-binding site and makes similar interactions with the catalytic residues. The structure suggests an explanation for the lower Michaelis-Menten constants at acidic pH. PubMed: 20516590DOI: 10.1107/S1744309110014259 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.35 Å) |
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