3CWG
Unphosphorylated mouse STAT3 core fragment
3CWG の概要
| エントリーDOI | 10.2210/pdb3cwg/pdb |
| 分子名称 | Signal transducer and activator of transcription 3 (1 entity in total) |
| 機能のキーワード | stat3, activator, acute phase, alternative splicing, cytoplasm, dna-binding, nucleus, phosphoprotein, sh2 domain, transcription, transcription regulation |
| 由来する生物種 | Mus musculus (Mouse) |
| 細胞内の位置 | Cytoplasm: P42227 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 128835.93 |
| 構造登録者 | Ren, Z.,Mao, X.,Mertens, C.,Krishnaraj, R.,Qin, J.,Mandal, P.K.,Romanowshi, M.J.,McMurray, J.S. (登録日: 2008-04-21, 公開日: 2008-07-01, 最終更新日: 2023-08-30) |
| 主引用文献 | Ren, Z.,Mao, X.,Mertens, C.,Krishnaraj, R.,Qin, J.,Mandal, P.K.,Romanowski, M.J.,McMurray, J.S.,Chen, X. Crystal structure of unphosphorylated STAT3 core fragment. Biochem.Biophys.Res.Commun., 374:1-5, 2008 Cited by PubMed Abstract: Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure. Solution studies further demonstrate that the core fragment of STAT3 is primarily monomeric. Mutations corresponding to those in STAT1, which lead to disruption of the core fragment interface and prolonged tyrosine phosphorylation, show little or no effect on the tyrosine phosphorylation kinetics of STAT3. These results highlight the structural and biochemical differences between STAT3 and STAT1, and suggest different regulation mechanisms of these two proteins. PubMed: 18433722DOI: 10.1016/j.bbrc.2008.04.049 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.05 Å) |
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