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Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1.,Ngo JC, Giang K, Chakrabarti S, Ma CT, Huynh N, Hagopian JC, Dorrestein PC, Fu XD, Adams JA, Ghosh G Mol Cell. 2008 Mar 14;29(5):563-76. PMID:18342604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Human
- Non-specific serine/threonine protein kinase
- Adams, J A.
- Chakrabarti, S.
- Dorrestein, P C.
- Fu, X D.
- Ghosh, G.
- Giang, K.
- Hagopian, J.
- Huynh, N.
- Ma, C T.
- Ngo, J C.
- Atp-binding
- Chromosome partition
- Differentiation
- Kinase
- Methylation
- Mrna processing
- Nucleotide-binding
- Nucleus
- Phosphoprotein
- Pre-mrna splicing
- Rna-binding
- Serine/threonine-protein kinase
- Spliceosome
- Sr protein
- Sr protein kinase
- Transferase
- Transferase-splicing complex