1szi
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(New page: 200px<br /><applet load="1szi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1szi, resolution 2.80Å" /> '''Crystal Structure of...)
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Revision as of 00:45, 21 November 2007
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Crystal Structure of the C-terminus of TIP47
Overview
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.
About this Structure
1SZI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of a lipid droplet protein; the PAT family member TIP47., Hickenbottom SJ, Kimmel AR, Londos C, Hurley JH, Structure. 2004 Jul;12(7):1199-207. PMID:15242596
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