2v3s

File:2v3s.gif

spinqualitylabelsall models 2v3s, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

OverviewOverview

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 ... [(full description)]

About this StructureAbout this Structure

2V3S is a [Protein complex] structure of sequences from [Homo sapiens] with ACT as [ligand]. Active as [Non-specific serine/threonine protein kinase], with EC number [2.7.11.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

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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