Literature summary for 2.7.10.1 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.

Search for more literature for 2.7.10.1

Activating Compound

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

Application

Application	Comment	Organism
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)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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
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
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
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]

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q08345	-	-

Source Tissue

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

Subunits

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

Synonyms

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

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Release 2023.1 (January 2023)