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      Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils.

      Nature
      Amino Acid Sequence, Animals, Base Sequence, Cattle, Cell Line, Cloning, Molecular, Collagen, DNA, genetics, Gene Expression, Lipoproteins, LDL, metabolism, Macromolecular Substances, Macrophages, analysis, Membrane Proteins, Molecular Sequence Data, Protein Conformation, Receptors, Immunologic, Receptors, Lipoprotein, Receptors, Scavenger, Scavenger Receptors, Class B

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          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.

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