A Sliding Docking Interaction Is Essential for Sequential and Processive Phosphorylation of an SR Protein by SRPK1
| Autor: | Nhat Huynh, Joseph A. Adams, Jonathan C. Hagopian, Kayla Giang, Pieter C. Dorrestein, Chen-Ting Ma, Xiang-Dong Fu, Jacky Chi Ki Ngo, Gourisankar Ghosh, Sutapa Chakrabarti |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Ribonucleoside Diphosphate Reductase Adenylyl Imidodiphosphate Molecular Sequence Data Plasma protein binding Protein Serine-Threonine Kinases Crystallography X-Ray environment and public health Article Substrate Specificity Serine Mice chemistry.chemical_compound SR protein Animals Humans Amino Acid Sequence Phosphorylation Binding site Molecular Biology Binding Sites Serine-Arginine Splicing Factors biology Nuclear Proteins RNA-Binding Proteins Active site Cell Biology Protein Structure Tertiary Biochemistry chemistry Docking (molecular) Multiprotein Complexes Phosphoserine biology.protein Biophysics Sequence Alignment Protein Binding |
| Zdroj: | Molecular Cell. 29(5):563-576 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2007.12.017 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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