Structural role of extracellular domain 1 of alpha-platelet-derived growth factor (PDGF) receptor for PDGF-AA and PDGF-BB binding

The purpose of this study was to bacterially express, purify, and refold combinations of the extracellular immunoglobulin (Ig)-like domains (2-3, 1-3, and 1-5) of the human alpha-platelet-derived growth factor receptor (alpha PDGFR) to characterize molecular interactions with its ligand, platelet-de...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 270; no. 46; pp. 27595 - 27600
Main Authors:	Mahadevan, D, Yu, J C, Saldanha, J W, Thanki, N, McPhie, P, Uren, A, LaRochelle, W J, Heidaran, M A
Format:	Journal Article
Language:	English
Published:	United States 17-11-1995
Subjects:	Becaplermin Binding Sites Chromatography, Affinity Circular Dichroism Extracellular Space - physiology Humans Iodine Radioisotopes Kinetics Models, Structural Platelet-Derived Growth Factor - metabolism Polymerase Chain Reaction Protein Conformation Protein Folding Proto-Oncogene Proteins c-sis Radioligand Assay Receptor, Platelet-Derived Growth Factor alpha Receptors, Platelet-Derived Growth Factor - chemistry Receptors, Platelet-Derived Growth Factor - isolation & purification Receptors, Platelet-Derived Growth Factor - metabolism Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping
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