Identification of residues in alpha-macroglobulins involved in activation of the alpha 2-macroglobulin signaling receptor.
Site-directed mutagenesis of residues in the receptor binding fragment of rat alpha 1-macroglobulin identify residues 1377 and 1378 (human numbering) as crucial for interaction with the alpha 2M signaling receptor on murine macrophages. Secondary structure prediction and signaling studies with the mutant proteins suggest the alpha 2M signaling receptor binding site involves part of a loop-helix-loop motif comprised of residues 1372-1378.
Howard
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Department of Pathology, Duke University Medical Center, Durham, NC 27710, USA.
DeCamp
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Misra
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Pizzo
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D003001:Cloning, Molecular; D018257:Helix-Loop-Helix Motifs; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D017737:Macrophages, Peritoneal / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D009154:Mutation / Q000235:genetics; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D051381:Rats; D011971:Receptors, Immunologic / Q000378:metabolism*; D015398:Signal Transduction / Q000235:genetics; D000511:alpha-Macroglobulins / Q000737:chemistry*
D026503:Low Density Lipoprotein Receptor-Related Protein-1; D010446:Peptide Fragments; D011971:Receptors, Immunologic; D000511:alpha-Macroglobulins; D002118:Calcium