1. Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils
- Author
-
Tatsuhiko Kodama, Monty Krieger, Paul Matsudaira, Lucia Rohrer, James Zabrecky, and Mason W. Freeman
- Subjects
Macromolecular Substances ,Protein Conformation ,Molecular Sequence Data ,Gene Expression ,Biology ,Cell Line ,Cell surface receptor ,Animals ,Amino Acid Sequence ,Scavenger receptor ,Cloning, Molecular ,Receptors, Immunologic ,Integral membrane protein ,Receptors, Lipoprotein ,Coiled coil ,chemistry.chemical_classification ,Receptors, Scavenger ,Multidisciplinary ,Base Sequence ,Macrophages ,Membrane Proteins ,DNA ,Scavenger Receptors, Class B ,Lipoproteins, LDL ,Transmembrane domain ,Macrophage receptor with collagenous structure ,Biochemistry ,chemistry ,Biophysics ,Cattle ,Collagen ,Glycoprotein ,Triple helix - Abstract
The macrophage scavenger receptor is a trimeric membrane glycoprotein with unusual ligand-binding properties which has been implicated in the development of atherosclerosis. The trimeric structure of the bovine type I scavenger receptor, deduced by complementary DNA cloning, contains three extracellular C-terminal cysteine-rich domains connected to the transmembrane domain by a long fibrous stalk. This stalk structure, composed of an alpha-helical coiled coil and a collagen-like triple helix, has not previously been observed in an integral membrane protein.
- Published
- 1990