2ehb: Difference between revisions

Revision as of 00:45, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ehb.png

Template:STRUCTURE 2ehb

The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3

Template:ABSTRACT PUBMED 17499048

About this StructureAbout this Structure

2EHB is a Protein complex structure of sequences from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 00:45:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3'''
+===The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17499048}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17499048 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17499048}}
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 [[Category: Signalling protein/transferase complex]]
 [[Category: Sos2 fisl motif]]
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