Multiple function of macrophage scavenger receptors mediated by fibrous coiled coil domains.
Type I and type II macrophage scavenger receptors (MSR) have six structurally distinct domains. MSR are known to mediate a wide range of ligand recognition, endocytosis, phagocytosis and macrophage adhesion. Expression of mutated receptors in various cultured cells and analysis using synthetic peptides indicate that two coiled-coil domains, alpha-helical coiled-coil domain (domain IV) and collagen-like domain (domain V) mediate these functions. Domain IV is essential for the trimerization of MSR and EDTA-resistant adhesion function. Domain V is essential for the wide range of ligand recognition. Cooperation of these two domains is also essential for the cellular function of MSR including pH-dependent ligand dissociation.
Liao
H S
HS
Third Department of Internal Medicine, University of Tokyo, Japan.
Doi
T
T
Wada
Y
Y
Matsumoto
A
A
Kodama
T
T
D000595:Amino Acid Sequence; D003094:Collagen / Q000235:genetics; D003196:Computer Graphics; D005796:Genes; D006801:Humans; D008957:Models, Genetic; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011971:Receptors, Immunologic / Q000235:genetics* / Q000378:metabolism*; D051116:Receptors, Scavenger
D011971:Receptors, Immunologic; D051116:Receptors, Scavenger; D003094:Collagen