3BEG
Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2
3BEG の概要
| エントリーDOI | 10.2210/pdb3beg/pdb |
| 分子名称 | Serine/threonine-protein kinase SRPK1, Splicing factor, arginine/serine-rich 1, PHOSPHOSERINE, ... (5 entities in total) |
| 機能のキーワード | kinase, sr protein kinase, sr protein, pre-mrna splicing, atp-binding, chromosome partition, differentiation, mrna processing, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, methylation, rna-binding, spliceosome, transferase-splicing complex, transferase/splicing |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Isoform 2: Cytoplasm. Isoform 1: Cytoplasm: Q96SB4 Cytoplasm : Q07955 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 57183.68 |
| 構造登録者 | Ngo, J.C.,Giang, K.,Chakrabarti, S.,Ma, C.-T.,Huynh, N.,Hagopian, J.,Dorrestein, P.C.,Fu, X.-D.,Adams, J.A.,Ghosh, G. (登録日: 2007-11-18, 公開日: 2008-04-01, 最終更新日: 2024-02-21) |
| 主引用文献 | Ngo, J.C.,Giang, K.,Chakrabarti, S.,Ma, C.-T.,Huynh, N.,Hagopian, J.,Dorrestein, P.C.,Fu, X.-D.,Adams, J.A.,Ghosh, G. A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1 Mol.Cell, 29:563-576, 2008 Cited by PubMed Abstract: The 2.9 A crystal structure of the core SRPK1:ASF/SF2 complex reveals that the N-terminal half of the basic RS domain of ASF/SF2, which is destined to be phosphorylated, is bound to an acidic docking groove of SRPK1 distal to the active site. Phosphorylation of ASF/SF2 at a single site in the C-terminal end of the RS domain generates a primed phosphoserine that binds to a basic site in the kinase. Biochemical experiments support a directional sliding of the RS peptide through the docking groove to the active site during phosphorylation, which ends with the unfolding of a beta strand of the RRM domain and binding of the unfolded region to the docking groove. We further suggest that the priming of the first serine facilitates directional substrate translocation and efficient phosphorylation. PubMed: 18342604DOI: 10.1016/j.molcel.2007.12.017 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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