Literature summary for 3.4.21.104 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00187	-	-

Subunits

Subunits	Comment	Organism
More	recombinant CUB1-EGF-CUB2 regions of MASP-2 show a slow and incomplete dissociation of dimer by EDTA and appearance of high molecular weight aggregates	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 thepresence 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

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Release 2023.1 (January 2023)