Type I macrophage scavenger receptor contains α-helical and collagen-like coiled coils
T Kodama, M Freeman, L Rohrer, J Zabrecky… - Nature, 1990 - nature.com
T Kodama, M Freeman, L Rohrer, J Zabrecky, P Matsudaira, M Krieger
Nature, 1990•nature.comThe 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 a-
helical coiled coil and a collagen-like triple helix, has not previously been observed in an …
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 a-
helical coiled coil and a collagen-like triple helix, has not previously been observed in an …
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 a-helical coiled coil and a collagen-like triple helix, has not previously been observed in an integral membrane protein.
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