2v3s

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[[Image:2v3s.gif|left|200px]]
[[Image:2v3s.gif|left|200px]]
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{{Structure
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|PDB= 2v3s |SIZE=350|CAPTION= <scene name='initialview01'>2v3s</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2v3s", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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{{STRUCTURE_2v3s| PDB=2v3s | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3s OCA], [http://www.ebi.ac.uk/pdbsum/2v3s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v3s RCSB]</span>
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'''STRUCTURAL INSIGHTS INTO THE RECOGNITION OF SUBSTRATES AND ACTIVATORS BY THE OSR1 KINASE'''
'''STRUCTURAL INSIGHTS INTO THE RECOGNITION OF SUBSTRATES AND ACTIVATORS BY THE OSR1 KINASE'''
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[[Category: Thastrup, J.]]
[[Category: Thastrup, J.]]
[[Category: Villa, F.]]
[[Category: Villa, F.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: magnesium]]
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[[Category: Magnesium]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:09:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:08 2008''
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Revision as of 15:09, 4 May 2008

Image:2v3s.gif

Template:STRUCTURE 2v3s

STRUCTURAL INSIGHTS INTO THE RECOGNITION OF SUBSTRATES AND ACTIVATORS BY THE OSR1 KINASE


Overview

The oxidative-stress-responsive kinase 1 (OSR1) and the STE20/SPS1-related proline/alanine-rich kinase (SPAK) are key enzymes in a signalling cascade regulating the activity of Na(+)/K(+)/2Cl(-) co-transporters (NKCCs) in response to osmotic stress. Both kinases have a conserved carboxy-terminal (CCT) domain, which recognizes a unique peptide (Arg-Phe-Xaa-Val) motif present in OSR1- and SPAK-activating kinases (with-no-lysine kinase 1 (WNK1) and WNK4) as well as its substrates (NKCC1 and NKCC2). Here, we describe the structural basis of this recognition event as shown by the crystal structure of the CCT domain of OSR1 in complex with a peptide containing this motif, derived from WNK4. The CCT domain forms a novel protein fold that interacts with the Arg-Phe-Xaa-Val motif through a surface-exposed groove. An intricate web of interactions is observed between the CCT domain and an Arg-Phe-Xaa-Val motif-containing peptide derived from WNK4. Mutational analysis shows that these interactions are required for the CCT domain to bind to WNK1 and NKCC1. The CCT domain structure also shows how phosphorylation of a Ser/Thr residue preceding the Arg-Phe-Xaa-Val motif results in a steric clash, promoting its dissociation from the CCT domain. These results provide the first molecular insight into the mechanism by which the SPAK and OSR1 kinases specifically recognize their upstream activators and downstream substrates.

About this Structure

2V3S is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural insights into the recognition of substrates and activators by the OSR1 kinase., Villa F, Goebel J, Rafiqi FH, Deak M, Thastrup J, Alessi DR, van Aalten DM, EMBO Rep. 2007 Sep;8(9):839-45. Epub 2007 Aug 17. PMID:17721439 Page seeded by OCA on Sun May 4 18:09:54 2008

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