1c8z: Difference between revisions

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<StructureSection load='1c8z' size='340' side='right'caption='[[1c8z]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1c8z' size='340' side='right'caption='[[1c8z]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c8z]] 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=1C8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C8Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c8z]] 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=1C8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C8Z FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1c8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8z OCA], [https://pdbe.org/1c8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c8z RCSB], [https://www.ebi.ac.uk/pdbsum/1c8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8z 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=1c8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8z OCA], [https://pdbe.org/1c8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c8z RCSB], [https://www.ebi.ac.uk/pdbsum/1c8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8z 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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c8z ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c8z ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tubby-like proteins (TULPs) are found in a broad range of multicellular organisms. In mammals, genetic mutation of tubby or other TULPs can result in one or more of three disease phenotypes: obesity (from which the name "tubby" is derived), retinal degeneration, and hearing loss. These disease phenotypes indicate a vital role for tubby proteins; however, no biochemical function has yet been ascribed to any member of this protein family. A structure-directed approach was employed to investigate the biological function of these proteins. The crystal structure of the core domain from mouse tubby was determined at a resolution of 1.9 angstroms. From primarily structural clues, experiments were devised, the results of which suggest that TULPs are a unique family of bipartite transcription factors.
Implication of tubby proteins as transcription factors by structure-based functional analysis.,Boggon TJ, Shan WS, Santagata S, Myers SC, Shapiro L Science. 1999 Dec 10;286(5447):2119-25. PMID:10591637<ref>PMID:10591637</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1c8z" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Boggon, T J]]
[[Category: Boggon TJ]]
[[Category: Myers, S C]]
[[Category: Myers SC]]
[[Category: Shapiro, L]]
[[Category: Shapiro L]]
[[Category: 12-stranded-beta-barrel]]
[[Category: Beta-barrel]]
[[Category: Deafness]]
[[Category: Filled-beta-roll]]
[[Category: Helix-filled-barrel]]
[[Category: Obesity blindness]]
[[Category: Signaling protein]]
[[Category: Tubby filled-barrel]]

Latest revision as of 09:41, 7 February 2024

C-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEINC-TERMINAL DOMAIN OF MOUSE BRAIN TUBBY PROTEIN

Structural highlights

1c8z is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ 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
  2. ↑ 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

1c8z, resolution 1.90Å

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