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9C8E

mouse Seipin complex

Summary for 9C8E
Entry DOI10.2210/pdb9c8e/pdb
Related9C8D
EMDB information45301 45302
DescriptorSeipin (1 entity in total)
Functional Keywordsseipin, lipid droplets, adipose, membrane protein
Biological sourceMus musculus (house mouse)
Total number of polymer chains11
Total formula weight560927.47
Authors
Li, C.,Han, Y.,Wynn, R.M.,Chen, Z.,Scherer, P.E. (deposition date: 2024-06-12, release date: 2025-08-27, Last modification date: 2025-11-19)
Primary citationLi, C.,Sun, X.N.,Funcke, J.B.,Vanharanta, L.,Prasanna, X.,Gov, K.,Li, Y.,Virostek, M.,Joung, C.,Joffin, N.,Kanerva, K.,Szkalisity, A.,Kulig, W.,Straub, L.,Chen, S.,Velasco, J.,Cobb, A.,La Padula, D.,Wang, M.Y.,Onodera, T.,Voros, C.,Kim, D.S.,Kim, M.,Varlamov, O.,Li, Y.,Liu, C.,Nawrocki, A.R.,Zhao, S.,Oh, D.Y.,Wang, Z.V.,Gordillo, R.,Goodman, J.M.,Wynn, R.M.,Henne, W.M.,Vattulainen, I.,Han, Y.,Ikonen, E.,Scherer, P.E.
Adipogenin promotes the development of lipid droplets by binding a dodecameric seipin complex.
Science, 390:eadr9755-eadr9755, 2025
Cited by
PubMed Abstract: The microprotein adipogenin (Adig) is predominantly expressed in adipose tissues. Here, we found that Adig interacts with seipin to form a stable, rigid complex. We present the structure of the seipin-Adig complex at an overall resolution of ~3.0 angstroms. The structure revealed that mammalian seipin assembles into two distinct oligomeric forms: undecamers and dodecamers. Adig selectively bound to the dodecameric form and enhanced seipin assembly by bridging and stabilizing adjacent subunits. Functionally, this complex promoted lipid droplet development at both early and late stages. In transgenic mice, adipocyte-specific overexpression of Adig increased fat mass and enlarged lipid droplets, whereas Adig deletion disrupted triglyceride accumulation in brown adipose tissues. Thus, Adig can modulate lipid storage through its structural and functional interactions with seipin.
PubMed: 41196993
DOI: 10.1126/science.adr9755
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.19 Å)
Structure validation

245663

数据于2025-12-03公开中

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