Analysis Biomolecular Interactions of TC and PC with PDGFRα on Fibroblasts by BLI (CAT#: STEM-MB-0242-CJ)

Introduction

PDGFRα is a type I transmembrane glycoprotein in the class III subfamily of receptor tyrosine kinases with a length of 1,089 bp and a molecular mass of 122,67 kDa. It is able to form homo- or heterodimeric receptors when disulphide-linked homodimers of Platelet Derived Growth Factor A, B, C or D or the heterodimer PDGFR-AB bind. In vivo PDGFRα mainly binds PDGF-AA and PDGF-CC. PDGFRα is activated by a de-repression of the tyrosine kinase activity. PDGFRα is expressed in most mesenchymal cells like in lung, skin and intestinal progenitor cells and in fibroblasts but not in endothelial and epithelial cells and induced by inflammation or growth in culture. It becomes active in stimulating cell-signalling pathways that trigger cellular growth and differentiation of certain tissues and organs during embryogenesis and the maintenance of these tissues during life.


Differences in the total amount and ratio of glycoprotein complexes have been detected in various HCMV strains, potentially influencing the variability in cellular tropism. Structural and biochemical characterization of HCMV TC and PC by mass spectrometry and mutagenesis analysis revealed that TC and PC form two mutually exclusive cell entry complexes. These complexes are formed by disulphide bonds between the cysteine 144 of gL and either the cysteine 351 of gO or the cysteine 162 of pUL128, meaning that both complexes use the same binding domain at the N terminus of gH/gL.