Literature summary for 3.4.21.104 extracted from

Drentin, N.; Conroy, P.; Gunzburg, M.J.; Pike, R.N.; Wijeyewickrema, L.C.
Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4 (2015), Mol. Immunol., 67, 287-293 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00187	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
C4 complement component + H2O	-	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
mannose-binding lectin-associated serine protease-2	-	Homo sapiens
MASP-2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	two areas outside of the active site of MASP-2 (so-called exosites) are crucial for efficient cleavage of substrate C4 complement component. Both exosites are required for high affinity binding and efficient cleavage of the substrate protein. Within the SP domain exosite, two arginine residues are most important for high affinity binding and efficient cleavage of C4. The CCP domain exosite appears to play the major role in the initial interaction with C4, whilst the SP domain exosite plays the major role in a secondary conformational change between the two proteins required to form a high affinity complex	Homo sapiens

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Release 2023.1 (January 2023)