1wbp: Difference between revisions
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|PDB= 1wbp |SIZE=350|CAPTION= <scene name='initialview01'>1wbp</scene>, resolution 2.40Å | |PDB= 1wbp |SIZE=350|CAPTION= <scene name='initialview01'>1wbp</scene>, resolution 2.40Å | ||
|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> | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=ADP:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''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
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| 1wbp, resolution 2.40Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | ACT and ADP | ||||||||||||
| 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- Protein complex
- Transferred entry: 2 7.11 1
- 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
