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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
|
| skos:exactMatch | |
| uniprot:name |
J. Biol. Chem.
|
| uniprot:author |
Bazan J.F.,
Fletterick R.J.,
Noland B.J.,
Pastuszyn A.,
Scallen T.J.
|
| uniprot:date |
1987
|
| uniprot:pages |
13219-13227
|
| uniprot:title |
Primary sequence and structural analysis of sterol carrier protein 2 from rat liver: homology with immunoglobulins.
|
| uniprot:volume |
262
|