2v3s

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[[Image:2v3s.gif|left|200px]]<br /><applet load="2v3s" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2v3s.gif|left|200px]]
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caption="2v3s, resolution 1.70&Aring;" />
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'''STRUCTURAL INSIGHTS INTO THE RECOGNITION OF SUBSTRATES AND ACTIVATORS BY THE OSR1 KINASE'''<br />
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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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|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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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURAL INSIGHTS INTO THE RECOGNITION OF SUBSTRATES AND ACTIVATORS BY THE OSR1 KINASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2V3S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3S OCA].
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2V3S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3S OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17721439 17721439]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17721439 17721439]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:42:58 2008''

Revision as of 16:43, 20 March 2008

Image:2v3s.gif


PDB ID 2v3s

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands:
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Coordinates: save as pdb, mmCIF, xml



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


Contents

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.

Disease

Known diseases associated with this structure: Pseudohypoaldosteronism type II OMIM:[601844]

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

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