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| | <StructureSection load='1i7e' size='340' side='right'caption='[[1i7e]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='1i7e' size='340' side='right'caption='[[1i7e]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1i7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1i7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IBS:L-ALPHA-GLYCEROPHOSPHO-D-MYO-INOSITOL-4,5-BIS-PHOSPHATE'>IBS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c8z|1c8z]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IBS:L-ALPHA-GLYCEROPHOSPHO-D-MYO-INOSITOL-4,5-BIS-PHOSPHATE'>IBS</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7e OCA], [https://pdbe.org/1i7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7e RCSB], [https://www.ebi.ac.uk/pdbsum/1i7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7e ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7e OCA], [https://pdbe.org/1i7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7e RCSB], [https://www.ebi.ac.uk/pdbsum/1i7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/TUB_MOUSE TUB_MOUSE]] Note=Defects in Tub are the cause of maturity-onset obesity, insulin resistance and sensory deficits.
| + | [https://www.uniprot.org/uniprot/TUB_MOUSE TUB_MOUSE] Note=Defects in Tub are the cause of maturity-onset obesity, insulin resistance and sensory deficits. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TUB_MOUSE TUB_MOUSE]] Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity).<ref>PMID:10591637</ref> <ref>PMID:11375483</ref>
| + | [https://www.uniprot.org/uniprot/TUB_MOUSE TUB_MOUSE] Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity).<ref>PMID:10591637</ref> <ref>PMID:11375483</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Baird, C L]] | + | [[Category: Baird CL]] |
| - | [[Category: Boggon, T J]] | + | [[Category: Boggon TJ]] |
| - | [[Category: Santagata, S]] | + | [[Category: Santagata S]] |
| - | [[Category: Shan, W S]] | + | [[Category: Shan WS]] |
| - | [[Category: Shapiro, L]] | + | [[Category: Shapiro L]] |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Tubby filled-barrel beta-barrel filled-beta-roll 12-stranded-beta-barrel helix-filled-barrel obesity blindness deafness phosphoinositide phosphatidylinositol]]
| + | |
| Structural highlights
Disease
TUB_MOUSE Note=Defects in Tub are the cause of maturity-onset obesity, insulin resistance and sensory deficits.
Function
TUB_MOUSE Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boggon TJ, Shan WS, Santagata S, Myers SC, Shapiro L. Implication of tubby proteins as transcription factors by structure-based functional analysis. Science. 1999 Dec 10;286(5447):2119-25. PMID:10591637
- ↑ Santagata S, Boggon TJ, Baird CL, Gomez CA, Zhao J, Shan WS, Myszka DG, Shapiro L. G-protein signaling through tubby proteins. Science. 2001 Jun 15;292(5524):2041-50. Epub 2001 May 24. PMID:11375483 doi:10.1126/science.1061233
- ↑ Santagata S, Boggon TJ, Baird CL, Gomez CA, Zhao J, Shan WS, Myszka DG, Shapiro L. G-protein signaling through tubby proteins. Science. 2001 Jun 15;292(5524):2041-50. Epub 2001 May 24. PMID:11375483 doi:10.1126/science.1061233
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