1wbp | pdb_00001wbp
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SRPK1 BOUND TO 9MER DOCKING MOTIF PEPTIDE
Overview
The arginine-serine (RS)-rich domain of the SR protein ASF/SF2 is, phosphorylated by SR protein kinases (SRPKs) and Clk/Sty kinases. However, the mode of phosphorylation by these kinases and their coordination in the, biological regulation of ASF/SF2 is unknown. Here, we report the crystal, structure of an active fragment of human SRPK1 bound to a peptide derived, from an SR protein. This structure led us to identify a docking motif in, ASF/SF2. We find that this docking motif restricts phosphorylation of, ASF/SF2 by SRPK1 to the N-terminal part of the RS domain - a property, essential for its assembly into nuclear speckles. We further show that, Clk/Sty causes release of ASF/SF2 from speckles by phosphorylating the, C-terminal part of its RS domain. These results suggest that the ... [(full description)]
About this Structure
1WBP is a [Protein complex] structure of sequences from [Homo sapiens] with ACT and ADP as [ligands]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].
Reference
Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2., Ngo JC, Chakrabarti S, Ding JH, Velazquez-Dones A, Nolen B, Aubol BE, Adams JA, Fu XD, Ghosh G, Mol Cell. 2005 Oct 7;20(1):77-89. PMID:16209947
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- Homo sapiens
- Protein complex
- Adams, J.A.
- Aubol, B.E.
- Chakrabarti, S.
- Ding, J.H.
- Fu, X.D.
- Ghosh, G.
- Ngo, J.C.
- Nolen, B.
- Velazquez-Dones, A.
- ACT
- ADP
- Alternative splicing
- Atp-binding
- Chromosome partition
- Differentiation
- Kinase
- Mrna processing
- Mrna splicing
- Nuclear protein
- Nucleotide-binding
- Phosphorylation
- Serine/threonine-protein kinase
- Srpk
- Transferase
