6ds5

From Proteopedia

Jump to: navigation, search

Cryo EM structure of human SEIPIN

Structural highlights

6ds5 is a 11 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:BSCL2 (HUMAN)
Experimental data:Check to display Experimental Data
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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

[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.[1] [2]

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Loading citation details..
Citations
reviews cite this structure
-1 more
other articles
No citations found

References

  1. ↑ Boutet E, El Mourabit H, Prot M, Nemani M, Khallouf E, Colard O, Maurice M, Durand-Schneider AM, Chretien Y, Gres S, Wolf C, Saulnier-Blache JS, Capeau J, Magre J. Seipin deficiency alters fatty acid Delta9 desaturation and lipid droplet formation in Berardinelli-Seip congenital lipodystrophy. Biochimie. 2009 Jun;91(6):796-803. doi: 10.1016/j.biochi.2009.01.011. Epub 2009, Feb 6. PMID:19278620 doi:http://dx.doi.org/10.1016/j.biochi.2009.01.011
  2. ↑ Tian Y, Bi J, Shui G, Liu Z, Xiang Y, Liu Y, Wenk MR, Yang H, Huang X. Tissue-autonomous function of Drosophila seipin in preventing ectopic lipid droplet formation. PLoS Genet. 2011 Apr;7(4):e1001364. doi: 10.1371/journal.pgen.1001364. Epub 2011 , Apr 14. PMID:21533227 doi:http://dx.doi.org/10.1371/journal.pgen.1001364
  3. ↑ Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H. Human SEIPIN Binds Anionic Phospholipids. Dev Cell. 2018 Oct 22;47(2):248-256.e4. doi: 10.1016/j.devcel.2018.09.010. Epub, 2018 Oct 4. PMID:30293840 doi:http://dx.doi.org/10.1016/j.devcel.2018.09.010

Contents


Downloading... [195024/446248]

6ds5, resolution 3.80Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://proteopedia.org/wiki/index.php/6ds5"
Personal tools