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Literature summary extracted from

  • Abdulhussein, R.; Koo, D.H.; Vogel, W.F.
    Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1 (2008), J. Biol. Chem., 283, 12026-12033.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.10.1 Collagen 250 kDa dimeric DDR1a entity is phosphorylated upon ligand stimulation Homo sapiens
2.7.10.1 additional information cysteines at position 303 and 348 are involved in covalent dimerization and/or ligand-induced receptor activation Homo sapiens

Application

EC Number Application Comment Organism
2.7.10.1 additional information existence of a disulfide-linked, dimeric form of DDR1 in human cells, which is activated upon collagen stimulation. Two cysteines in the stalk region of the receptor are most likely necessary not only for the formation of covalent dimers but also for proper receptor post-translational maturation Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.10.1 MCF-7 cells stably transfected with a mammalian expression vector pIRES-Neo containing the FLAG-tagged human cDNA of DDR1 isoforms a and d. 293 cells transfected with plasmids coding for HA-tagged DDR1a and DDR1d. Mutant constructs expressed in 293 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.10.1 C289S strong ligand-triggered phosphorylation as for the wild-type DDR1. In the absence of beta-mercaptoethanol, forms dimers (250 kDa). Binds to immobilized collagen at comparable levels as the wild-type. DDR1b and C289S constructs bind to collagen-agarose beads equally well Homo sapiens
2.7.10.1 C303S no ligand-triggered phosphorylation. In the absence of beta-mercaptoethanol, does not form dimers. Has a significantly lower affinity to bind to immobilized collagen, relative to wild type DDR1. Shows no affinity to collagen-agarose beads Homo sapiens
2.7.10.1 C348S no ligand-triggered phosphorylation. In the absence of beta-mercaptoethanol, does not form dimers. Has a significantly lower affinity to bind to immobilized collagen, relative to wild type DDR1. Shows no affinity to collagen-agarose beads Homo sapiens
2.7.10.1 additional information DDR1 mutants lacking the stalk region fail to form dimers, whereas deletion of the discoidin domain does not prevent dimerization Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.10.1 125000
-
 Western blot analysis, under reducing conditions Homo sapiens
2.7.10.1 250000
-
 Western blot analysis, under nonreducing conditions Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.10.1 Homo sapiens Q08345
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.10.1 T-47D cell
-
 Homo sapiens
-

Subunits

EC Number Subunits Comment Organism
2.7.10.1 dimer SDS-PAGE, both a monomer and 250 kDa dimer under nonreducing conditions, 125 kDa monomeric protein under reducing conditions Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.10.1 DDR1
-
 Homo sapiens
2.7.10.1 discoidin domain receptor 1
-
 Homo sapiens
2.7.10.1 receptor tyrosine kinase
-
 Homo sapiens