Structure of the Discoidin Domain Receptor 1 Extracellular Region Bound to an Inhibitory Fab Fragment Reveals Features Important for Signaling

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...

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Veröffentlicht in:	Structure (London) 2012-04, Vol.20 (4), p.688-697
Hauptverfasser:	Carafoli, Federico, Mayer, Marie Cathrin, Shiraishi, Kazushige, Pecheva, Mira Anguelova, Chan, Lai Yi, Nan, Ruodan, Leitinger, Birgit, Hohenester, Erhard
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Neutralizing - chemistry Binding Sites Collagen - chemistry Collagen - genetics Crystallography, X-Ray Discoidin Domain Receptor 1 Discoidin Domain Receptors Flow Cytometry HEK293 Cells Humans Immunoglobulin Fab Fragments - chemistry Models, Molecular Protein Binding Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Protein Subunits - antagonists & inhibitors Protein Subunits - chemistry Protein Subunits - genetics Receptor Protein-Tyrosine Kinases - antagonists & inhibitors Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - genetics Receptors, Mitogen - chemistry Receptors, Mitogen - genetics Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Signal Transduction - genetics Transfection
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