2ehb
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(New page: 200px<br /><applet load="2ehb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ehb, resolution 2.10Å" /> '''The structure of the...)
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Revision as of 11:25, 23 January 2008
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The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
Overview
The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding, calcium signals elicited by different environmental stimuli. SOS2 is, activated by Ca-SOS3 and subsequently phosphorylates the ion transporter, SOS1 to bring about cellular ion homeostasis under salt stress. In, addition to possessing the kinase activity, members of the SOS2 family of, protein kinases can bind to protein phosphatase 2Cs. The crystal structure, of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of, SOS2 resolves central questions regarding the dual function of SOS2 as a, kinase and a phosphatase-binding protein. A comparison with the structure, of unbound SOS3 reveals the basis of the molecular function of this family, of kinases and their interacting calcium sensors. Furthermore, our study, suggests that the structure of the phosphatase-interaction domain of SOS2, defines a scaffold module conserved from yeast to human.
About this Structure
2EHB is a Protein complex structure of sequences from Arabidopsis thaliana with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3., Sanchez-Barrena MJ, Fujii H, Angulo I, Martinez-Ripoll M, Zhu JK, Albert A, Mol Cell. 2007 May 11;26(3):427-35. PMID:17499048
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