1o6u | pdb_00001o6u
THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
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Overview
Supernatant protein factor (SPF) promotes the epoxidation of squalene, catalyzed by microsomes. Several studies suggest its in vivo role in the, cholesterol biosynthetic pathway by a yet unknown mechanism. SPF belongs, to a family of lipid binding proteins called CRAL_TRIO, which include, yeast phosphatidylinositol transfer protein Sec14 and tocopherol transfer, protein TTP. The crystal structure of human SPF at a resolution of 1.9 A, reveals a two domain topology. The N-terminal 275 residues form a, Sec14-like domain, while the C-terminal 115 residues consist of an, eight-stranded jelly-roll barrel similar to that found in many viral, protein structures. The ligand binding cavity has a peculiar, horseshoe-like shape. Contrary to the Sec14 crystal structure, the, lipid-exchange loop is in ... [(full description)]
About this Structure
1O6U is a [Single protein] structure of sequence from [Homo sapiens] with PLM as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the human supernatant protein factor., Stocker A, Tomizaki T, Schulze-Briese C, Baumann U, Structure. 2002 Nov;10(11):1533-40. PMID:12429094
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