Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2: identification of collagen binding sites in DDR2
B Leitinger - Journal of Biological Chemistry, 2003 - ASBMB
The widely expressed mammalian discoidin domain receptors (DDRs), DDR1 and DDR2,
are unique among receptor tyrosine kinases in that they are activated by the extracellular
matrix protein collagen. Various collagen types bind to and activate the DDRs, but the
molecular details of collagen recognition have not been well defined. In this study,
recombinant extracellular domains of DDR1 and DDR2 were produced to explore DDR-
collagen binding in detail. In solid phase assays, both DDRs bound collagen I with high …
are unique among receptor tyrosine kinases in that they are activated by the extracellular
matrix protein collagen. Various collagen types bind to and activate the DDRs, but the
molecular details of collagen recognition have not been well defined. In this study,
recombinant extracellular domains of DDR1 and DDR2 were produced to explore DDR-
collagen binding in detail. In solid phase assays, both DDRs bound collagen I with high …
