1o6u
From Proteopedia
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THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
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
Page seeded by OCA on Mon Oct 29 16:55:38 2007
