3ont: Difference between revisions
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==The Crystal Structure of Spot14, a modulator of lipogenesis== | ==The Crystal Structure of Spot14, a modulator of lipogenesis== | ||
<StructureSection load='3ont' size='340' side='right' caption='[[3ont]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='3ont' size='340' side='right'caption='[[3ont]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ont]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ont]] 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=3ONT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ont FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ont OCA], [https://pdbe.org/3ont PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ont RCSB], [https://www.ebi.ac.uk/pdbsum/3ont PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ont ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/THRSP_MOUSE THRSP_MOUSE] Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA. May function as transcriptional coactivator. May modulate the transcription factor activity of THRB (By similarity).<ref>PMID:15890771</ref> <ref>PMID:20952656</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ont" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Colbert | [[Category: Colbert CL]] | ||
[[Category: Deisenhofer | [[Category: Deisenhofer J]] | ||
[[Category: Kwon | [[Category: Kwon HJ]] | ||
Latest revision as of 12:31, 30 October 2024
The Crystal Structure of Spot14, a modulator of lipogenesisThe Crystal Structure of Spot14, a modulator of lipogenesis
Structural highlights
FunctionTHRSP_MOUSE Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA. May function as transcriptional coactivator. May modulate the transcription factor activity of THRB (By similarity).[1] [2] Publication Abstract from PubMedSpot 14 (S14) is a protein that is abundantly expressed in lipogenic tissues and is regulated in a manner similar to other enzymes involved in fatty acid synthesis. Deletion of S14 in mice decreased lipid synthesis in lactating mammary tissue, but the mechanism of S14's action is unknown. Here we present the crystal structure of S14 to 2.65 A and biochemical data showing that S14 can form heterodimers with MIG12. MIG12 modulates fatty acid synthesis by inducing the polymerization and activity of acetyl-CoA carboxylase, the first committed enzymatic reaction in the fatty acid synthesis pathway. Coexpression of S14 and MIG12 leads to heterodimers and reduced acetyl-CoA carboxylase polymerization and activity. The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG12 to activate ACC. Crystal structure of Spot 14, a modulator of fatty acid synthesis.,Colbert CL, Kim CW, Moon YA, Henry L, Palnitkar M, McKean WB, Fitzgerald K, Deisenhofer J, Horton JD, Kwon HJ Proc Natl Acad Sci U S A. 2010 Nov 2;107(44):18820-5. Epub 2010 Oct 15. PMID:20952656[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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