Ontology highlight
ABSTRACT:
SUBMITTER: Carafoli F
PROVIDER: S-EPMC3320712 | biostudies-literature | 2012 Apr
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20120403 4
The discoidin domain receptors, DDR1 and DDR2, are constitutively dimeric receptor tyrosine kinases that are activated by triple-helical collagen. Aberrant DDR signaling contributes to several human pathologies, including many cancers. We have generated monoclonal antibodies (mAbs) that inhibit DDR1 signaling without interfering with collagen binding. The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin ...[more]