Primary sequence and structural analysis of sterol carrier protein 2 from rat liver: homology with immunoglobulins

Sterol carrier protein 2 (SCP2) is involved in the later steps of cholesterol biosynthesis and in the intracellular transport of cholesterol. In the present investigation, the amino acid sequence of SCP2 from rat liver has been determined. It is a single polypeptide chain with 122 amino acid residue...

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Veröffentlicht in:The Journal of biological chemistry 1987-09, Vol.262 (27), p.13219-13227
Hauptverfasser: Pastuszyn, A, Noland, B J, Bazan, J F, Fletterick, R J, Scallen, T J
Format: Artikel
Sprache:eng
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Zusammenfassung:Sterol carrier protein 2 (SCP2) is involved in the later steps of cholesterol biosynthesis and in the intracellular transport of cholesterol. In the present investigation, the amino acid sequence of SCP2 from rat liver has been determined. It is a single polypeptide chain with 122 amino acid residues. Secondary structure prediction indicates an amphipathic alpha-helix region for residues 21-34 and antiparallel beta-sheet structure for residues 35-95. A major finding is the significant homology which exists over approximately 80 residues between SCP2 and the variable domains of the heavy chain of immunoglobulin G.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)45190-3