Two PDGF‐B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation

PDGF may be involved in the pathogenesis of a variety of disorders including atherosclerosis and certain types of cancer. There is currently little understanding of the molecular structure of PDGF and of the critical amino acid residues involved in receptor binding and cell activation. Two such PDGF...

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Bibliographic Details
Published in:The EMBO journal 1991-12, Vol.10 (13), p.4113-4120
Main Authors: Clements, J.M., Bawden, L.J., Bloxidge, R.E., Catlin, G., Cook, A.L., Craig, S., Drummond, A.H., Edwards, R.M., Fallon, A., Green, D.R.
Format: Article
Language:English
Subjects:
3T3 Cells
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Arginine - metabolism
Biological and medical sciences
Circular Dichroism
Enzyme-Linked Immunosorbent Assay
Fluorescence Polarization
Fundamental and applied biological sciences. Psychology
Inositol - metabolism
Isoleucine - metabolism
Mice
Mitogens
Molecular Sequence Data
Mutation
Plasmids
Platelet-Derived Growth Factor - metabolism
Protein hormones. Growth factors. Cytokines
Proteins
Receptors, Cell Surface - metabolism
Receptors, Platelet-Derived Growth Factor
site-directed mutagenesis
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Summary:PDGF may be involved in the pathogenesis of a variety of disorders including atherosclerosis and certain types of cancer. There is currently little understanding of the molecular structure of PDGF and of the critical amino acid residues involved in receptor binding and cell activation. Two such PDGF‐B chain residues, arginine 27 and isoleucine 30, have been identified by a site‐directed mutagenesis programme. Substitutions in these positions can lead to PDGF mutants defective in both receptor affinity and cell activation as judged by displacement of [125I]PDGF‐BB, mitogenic assay and inositol lipid turnover. Circular dichroism and fluorescence spectroscopy show that such mutations do not disrupt the structure of PDGF.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1991.tb04988.x