1wbp

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spinqualitylabelsall models 1wbp, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 docking, motif of ASF/SF2 is a key regulatory element for sequential, phosphorylation by SRPK1 and Clk/Sty and, thus, is essential for its, subcellular localization.

About this Structure

1WBP is a Protein complex structure of sequences from Homo sapiens with ACT and ADP as ligands. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Structure known Active Site: AC1. 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

Page seeded by OCA on Mon Nov 5 13:49:23 2007