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Structural Role of Extracellular Domain 1 of α-Platelet-derived Growth Factor (PDGF) Receptor for PDGF-AA and PDGF-BB Binding
Journal of Biological Chemistry
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 ␣-platelet-derived growth factor receptor (␣PDGFR) to characterize molecular interactions with its ligand, platelet-derived growth factor (PDGF). The far UV circular dichroism spectroscopy of the ␣-PDGFR extracellular domains (ECDs) revealed a predominantly ␤-sheet protein, with a structure consistent with folded Ig-likedoi:10.1074/jbc.270.46.27595 pmid:7499222 fatcat:3it2jepv3bhmpcw7avjltcfc6q