1SZI

Crystal Structure of the C-terminus of TIP47

Summary for 1SZI

• Entry DOI: 10.2210/pdb1szi/pdb
• Descriptor: mannose-6-phosphate receptor binding protein 1 (1 entity in total)
• Functional Keywords: 4-helix bundle, alpha/beta domain, pat protein, lipid binding, peptide binding
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm : Q9DBG5
• Total number of polymer chains: 1
• Total formula weight: 27569.86

Authors

Hickenbottom, S.J.,Kimmel, A.R.,Londos, C.,Hurley, J.H. (deposition date: 2004-04-05, release date: 2004-07-27, Last modification date: 2024-02-14)

Primary citation

Hickenbottom, S.J.,Kimmel, A.R.,Londos, C.,Hurley, J.H.
Structure of a Lipid Droplet Protein: The PAT Family Member TIP47
Structure, 12:1199-1207, 2004

PubMed Abstract: The perilipin/ADRP/TIP47 (PAT) proteins localize to the surface of intracellular neutral lipid droplets. Perilipin is essential for lipid storage and hormone regulated lipolysis in adipocytes, and perilipin null mice exhibit a dramatic reduction in adipocyte lipid stores. A significant fraction of the approximately 200 amino acid N-terminal region of the PAT proteins consists of 11-mer helical repeats that are also found in apolipoproteins and other lipid-associated proteins. The C-terminal 60% of TIP47, a representative PAT protein, comprises a monomeric and independently folded unit. The crystal structure of the C-terminal portion of TIP47 was determined and refined at 2.8 A resolution. The structure consists of an alpha/beta domain of novel topology and a four-helix bundle resembling the LDL receptor binding domain of apolipoprotein E. The structure suggests an analogy between PAT proteins and apolipoproteins in which helical repeats interact with lipid while the ordered C-terminal region is involved in protein:protein interactions.

PubMed: 15242596
DOI: 10.1016/j.str.2004.04.021

Experimental method

X-RAY DIFFRACTION (2.8 Å)