[HTML][HTML] Characterization of High Affinity Binding Motifs for the Discoidin Domain Receptor DDR2 in Collagen*♦
AD Konitsiotis, N Raynal, D Bihan, E Hohenester… - Journal of biological …, 2008 - ASBMB
The discoidin domain receptors, DDR1 and DDR2, are receptor tyrosine kinases that are
activated by native triple-helical collagen. Here we have located three specific DDR2
binding sites by screening the entire triple-helical domain of collagen II, using the Collagen II
Toolkit, a set of overlapping triple-helical peptides. The peptide sequence that bound DDR2
with highest affinity interestingly contained the sequence for the high affinity binding site for
von Willebrand factor in collagen III. Focusing on this sequence, we used a set of truncated …
activated by native triple-helical collagen. Here we have located three specific DDR2
binding sites by screening the entire triple-helical domain of collagen II, using the Collagen II
Toolkit, a set of overlapping triple-helical peptides. The peptide sequence that bound DDR2
with highest affinity interestingly contained the sequence for the high affinity binding site for
von Willebrand factor in collagen III. Focusing on this sequence, we used a set of truncated …