6ds5
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | The entry | + | ==Cryo EM structure of human SEIPIN== |
+ | <StructureSection load='6ds5' size='340' side='right' caption='[[6ds5]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6ds5]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DS5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DS5 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ds5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ds5 OCA], [http://pdbe.org/6ds5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ds5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ds5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ds5 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [[http://www.uniprot.org/uniprot/BSCL2_HUMAN BSCL2_HUMAN]] Autosomal dominant spastic paraplegia type 17;Severe neurodegenerative syndrome with lipodystrophy;Distal hereditary motor neuropathy type 5;Berardinelli-Seip congenital lipodystrophy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/BSCL2_HUMAN BSCL2_HUMAN]] Is a regulator of lipid catabolism essential for adipocyte differentiation. May also be involved in the central regulation of energy homeostasis (By similarity). Necessary for correct lipid storage and lipid droplets maintenance; may play a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues.<ref>PMID:19278620</ref> <ref>PMID:21533227</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a critical role in both LD formation and adipogenesis. The molecular function of SEIPIN, however, has yet to be elucidated. Here, we report the cryogenic electron microscopy structure of human SEIPIN at 3.8 A resolution. SEIPIN exists as an undecamer, and this oligomerization state is critical for its physiological function. The evolutionarily conserved lumenal domain of SEIPIN forms an eight-stranded beta sandwich fold. Both full-length SEIPIN and its lumenal domain can bind anionic phospholipids including phosphatidic acid. Our results suggest that SEIPIN forms a scaffold that helps maintain phospholipid homeostasis and surface tension of the ER. | ||
- | + | Human SEIPIN Binds Anionic Phospholipids.,Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H Dev Cell. 2018 Oct 22;47(2):248-256.e4. doi: 10.1016/j.devcel.2018.09.010. Epub, 2018 Oct 4. PMID:30293840<ref>PMID:30293840</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6ds5" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Qian, H W]] | ||
+ | [[Category: Yan, N]] | ||
+ | [[Category: Yan, R H]] | ||
+ | [[Category: Yang, H Y]] | ||
+ | [[Category: Adipogenesis]] | ||
+ | [[Category: Lipid binding protein]] | ||
+ | [[Category: Lipid droplet]] |
Revision as of 05:54, 24 October 2018
Cryo EM structure of human SEIPIN
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