3DAK

Crystal Structure of Domain-Swapped OSR1 kinase domain

Summary for 3DAK

• Entry DOI: 10.2210/pdb3dak/pdb
• Descriptor: Serine/threonine-protein kinase OSR1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: serine/threonine protein kinase, ste20, domain-swapping, atp-binding, kinase, magnesium, metal-binding, nucleotide-binding, phosphoprotein, polymorphism, serine/threonine-protein kinase, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : O95747
• Total number of polymer chains: 4
• Total formula weight: 131836.56

Authors

Lee, S.,Cobb, M.H.,Goldsmith, E.J. (deposition date: 2008-05-29, release date: 2009-02-10, Last modification date: 2024-02-21)

Primary citation

Lee, S.J.,Cobb, M.H.,Goldsmith, E.J.
Crystal structure of domain-swapped STE20 OSR1 kinase domain.
Protein Sci., 18:304-313, 2008

PubMed Abstract: OSR1 (oxidative stress-responsive-1) and SPAK (Ste20/Sps1-related proline/alanine-rich kinase) belong to the GCK-VI subfamily of Ste20 group kinases. OSR1 and SPAK are key regulators of NKCCs (Na(+)/K(+)/2Cl(-) cotransporters) and activated by WNK family members (with-no-lysine kinase), mutations of which are known to cause Gordon syndrome, an autosomal dominant form of inherited hypertension. The crystal structure of OSR1 kinase domain has been solved at 2.25 A. OSR1 forms a domain-swapped dimer in an inactive conformation, in which P+1 loop and alphaEF helix are swapped between dimer-related monomers. Structural alignment with nonswapped Ste20 TAO2 kinase indicates that the integrity of chemical interactions in the kinase domain is well preserved in the domain-swapped interfaces. The OSR1 kinase domain has now been added to a growing list of domain-swapped protein kinases recently reported, suggesting that the domain-swapping event provides an additional layer of complexity in regulating protein kinase activity.

PubMed: 19177573
DOI: 10.1002/pro.27

Experimental method

X-RAY DIFFRACTION (2.25 Å)