4MAC

Crystal structure of CIDE-N domain of FSP27

Summary for 4MAC

• Entry DOI: 10.2210/pdb4mac/pdb
• Descriptor: Cell death activator CIDE-3 (2 entities in total)
• Functional Keywords: roll fold, protein interaction, perilipin1, apoptosis
• Biological source: Mus musculus (mouse)
• Cellular location: Lipid droplet: P56198
• Total number of polymer chains: 2
• Total formula weight: 22548.17

Authors

Park, H.H.,Lee, S.M. (deposition date: 2013-08-16, release date: 2014-07-02, Last modification date: 2024-03-20)

Primary citation

Lee, S.M.,Jang, T.H.,Park, H.H.
Molecular basis for homo-dimerization of the CIDE domain revealed by the crystal structure of the CIDE-N domain of FSP27
Biochem.Biophys.Res.Commun., 439:564-569, 2013

PubMed Abstract: FSP27 (CIDE-3 in humans) plays critical roles in lipid metabolism and apoptosis and is known to be involved in regulation of lipid droplet (LD) size and lipid storage and apoptotic DNA fragmentation. Given that CIDE-containing proteins including FSP27 are associated with many human diseases including cancer, aging, diabetes, and obesity, studies of FSP27 and other CIDE-containing proteins are of great biological importance. As a first step toward elucidating the molecular mechanisms of FSP27-mediated lipid droplet growth and apoptosis, we report the crystal structure of the CIDE-N domain of FSP27 at a resolution of 2.0 Å. The structure revealed a possible biologically important homo-dimeric interface similar to that formed by the hetero-dimeric complex, CAD/ICAD. Comparison with other structural homologues revealed that the PB1 domain of BEM1P, ubiquitin-like domain of BAG6 and ubiquitin are structurally similar proteins. Our homo-dimeric structure of the CIDE-N domain of FSP27 will provide important information that will enable better understanding of the function of FSP27.

PubMed: 24025675
DOI: 10.1016/j.bbrc.2013.09.018

Experimental method

X-RAY DIFFRACTION (2 Å)