Coiled-coil fibrous domains mediate ligand binding by macrophage scavenger receptor type II (original) (raw)
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- Published: 08 February 1990
Nature volume 343, pages 570–572 (1990)Cite this article
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Abstract
THE macrophage scavenger receptor, which has been implicated in the pathogenesis of atherosclerosis1,2, has an unusually broad binding specificity1. Ligands include modified low-density lipoprotein and some polyanions (for example, poly(I) but not poly(C)). The scavenger receptor type I (ref. 3) has three principal extracellular domains that could participate in ligand binding: two fibrous coiled-coil domains (α-helical coiled-coil domain IV and collagen-like domain V), and the 110-amino-acid cysteine-rich C-terminal domain VI. We have cloned complementary DNAs encoding a second scavenger receptor which we have termed type II. This receptor is identical to the type I receptor, except that the cysteine-rich domain is replaced by a six-residue C terminus. Despite this truncation, the type II receptor mediates endocytosis of chemically modified low-density lipoprotein with high affinity and specificity, similar to that of the type I receptor. Therefore one or both of the extracellular fibrous domains are responsible for the unusual ligand-binding specificity of the receptor.
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Authors and Affiliations
- Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02168, USA
Lucia Rohrer, Mason Freeman, Tatsuhiko Kodama, Marsha Penman & Monty Krieger - Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts, 02114, USA
Mason Freeman
Authors
- Lucia Rohrer
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Rohrer, L., Freeman, M., Kodama, T. et al. Coiled-coil fibrous domains mediate ligand binding by macrophage scavenger receptor type II.Nature 343, 570–572 (1990). https://doi.org/10.1038/343570a0
- Received: 15 December 1989
- Accepted: 05 January 1990
- Issue Date: 08 February 1990
- DOI: https://doi.org/10.1038/343570a0