Structure (London), 2002-11, Vol.10 (11), p.1533-1540
2002
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- Autor(en) / Beteiligte
- Titel
- Crystal Structure of the Human Supernatant Protein Factor
- Ist Teil von
- Structure (London), 2002-11, Vol.10 (11), p.1533-1540
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2002
- Quelle
- Access via ScienceDirect (Elsevier)
- Beschreibungen/Notizen
- 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 Å 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 a closed conformation, suggesting a mechanism for lipid exchange.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0969-2126eISSN: 1878-4186DOI: 10.1016/S0969-2126(02)00884-5Titel-ID: cdi_proquest_miscellaneous_72690980
- Format
- –
- Schlagworte
- Carrier Proteins - chemistry, cral_trio, crystal structure, Crystallography, X-Ray, Humans, Ligands, Lipid Metabolism, Lipoproteins - chemistry, Models, Molecular, phosphatidylinositol transfer protein, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Spectrometry, Mass, Electrospray Ionization, squalene, tocopherol, Trans-Activators