Literature summary for 3.4.21.B7 extracted from

Parej, K.; Hermann, A.; Donath, N.; Zavodszky, P.; Gal, P.; Dobo, J.
Dissociation and re-association studies on the interaction domains of mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, provide evidence for heterodimer formation (2014), Mol. Immunol., 59, 1-9.

Search for more literature for 3.4.21.B7

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens
expression of chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 construct in Escherichia coli strain BL21 (DE3) pLysS in inclusion bodies	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a truncated enzyme version comprising the MAPS-1 CUB1-EGF-CUB2 domains, i.e. MASP-1 D1-3 CBD, rapid dissociation upon EDTA treatment, and heterodimer formation, exchange of subunits between dimers in the presence of Ca2+, overview. Heterodimer formation between N-terminal fragemnts of MASP1 and MASP-2, i.e. MASP-1 D1-3 and MASP-2 D1-3, is structurally allowed but takes place to only a small amount	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	required, enzyme-bound	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P48740	-	-

Purification (Commentary)

Purification (Comment)	Organism
refolded recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 by anion echange chromatography and gel filtration	Homo sapiens

Renatured (Commentary)

Renatured (Comment)	Organism
solubilization of recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 from Escherichia coli strain BL21 (DE3) pLysS inclusion bodies by 7 M guanidinium hydrochloride in 50 mM Tris, 50 mM DTT, pH 8.0, followed by dilution to 5.5 mg/ml protein, and refolding by diluting 20 ml of the 5 mg/mL solution into 1 l of 0.75 M Arg, 200 mM CaCl2, 3 mM glutathione, 2 mM oxidized glutathione, pH 8.0, refolding buffer, at least one week at 4°C, followed by dialysis	Homo sapiens

Renatured (Comment)

Organism

solubilization of recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 from Escherichia coli strain BL21 (DE3) pLysS inclusion bodies by 7 M guanidinium hydrochloride in 50 mM Tris, 50 mM DTT, pH 8.0, followed by dilution to 5.5 mg/ml protein, and refolding by diluting 20 ml of the 5 mg/mL solution into 1 l of 0.75 M Arg, 200 mM CaCl2, 3 mM glutathione, 2 mM oxidized glutathione, pH 8.0, refolding buffer, at least one week at 4°C, followed by dialysis

Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood plasma	-	Homo sapiens	-

Subunits

Subunits	Comment	Organism
dimer	the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain	Homo sapiens
More	in buffer containing EDTA, MASP-1 regions D1-3 dissociate slowly to monomers. Upon re-calcification dimers are re-formed, but this process is even slower	Homo sapiens

Synonyms

Synonyms	Comment	Organism
MASP-1	-	Homo sapiens
MBL-associated serine protease 1	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	mannan-binding lectin-associated serine proteases MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in the presence of Ca2+ exchange of subunits is slow between the homodimers. Modeling of isoforms MASP-1:MASP-3 heterodimer formation indicates that subunits of these proteins are readily exchanged even in the presence of Ca2+	Homo sapiens