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

Nature. 1990 Feb 8;343(6258):531-5. doi: 10.1038/343531a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 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* / genetics
  • Receptors, Lipoprotein*
  • Receptors, Scavenger
  • Scavenger Receptors, Class B


  • Lipoproteins, LDL
  • Macromolecular Substances
  • Membrane Proteins
  • Receptors, Immunologic
  • Receptors, Lipoprotein
  • Receptors, Scavenger
  • Scarb1 protein, mouse
  • Scavenger Receptors, Class B
  • acetyl-LDL
  • Collagen
  • DNA