1i7e
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(New page: 200px<br /><applet load="1i7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i7e, resolution 1.95Å" /> '''C-Terminal Domain Of...)
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Revision as of 15:00, 20 November 2007
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C-Terminal Domain Of Mouse Brain Tubby Protein bound to Phosphatidylinositol 4,5-bis-phosphate
Overview
Dysfunction of the tubby protein results in maturity-onset obesity in, mice. Tubby has been implicated as a transcription regulator, but details, of the molecular mechanism underlying its function remain unclear. Here we, show that tubby functions in signal transduction from heterotrimeric, GTP-binding protein (G protein)-coupled receptors. Tubby localizes to the, plasma membrane by binding phosphatidylinositol 4,5-bisphosphate through, its carboxyl terminal "tubby domain." X-ray crystallography reveals the, atomic-level basis of this interaction and implicates tubby domains as, phosphorylated-phosphatidyl- inositol binding factors. Receptor-mediated, activation of G protein alphaq (Galphaq) releases tubby from the plasma, membrane through the action of phospholipase C-beta, triggering, translocation of tubby to the cell nucleus. The localization of tubby-like, protein 3 (TULP3) is similarly regulated. These data suggest that tubby, proteins function as membrane-bound transcription regulators that, translocate to the nucleus in response to phosphoinositide hydrolysis, providing a direct link between G-protein signaling and the regulation of, gene expression.
About this Structure
1I7E is a Single protein structure of sequence from Mus musculus with IBS as ligand. Full crystallographic information is available from OCA.
Reference
G-protein signaling through tubby proteins., Santagata S, Boggon TJ, Baird CL, Gomez CA, Zhao J, Shan WS, Myszka DG, Shapiro L, Science. 2001 Jun 15;292(5524):2041-50. Epub 2001 May 24. PMID:11375483
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