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1wbp

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|PDB= 1wbp |SIZE=350|CAPTION= <scene name='initialview01'>1wbp</scene>, resolution 2.40&Aring;
|PDB= 1wbp |SIZE=350|CAPTION= <scene name='initialview01'>1wbp</scene>, resolution 2.40&Aring;
|SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]
|GENE=
|GENE=
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:05:52 2008''

Revision as of 12:05, 23 March 2008

Image:1wbp.gif


PDB ID 1wbp

Drag the structure with the mouse to rotate
, resolution 2.40Å
Sites:
Ligands: and
Activity: Transferred entry: 2.7.11.1, with EC number 2.7.1.37
Coordinates: save as pdb, mmCIF, xml



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. 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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