Literature summary for 3.4.21.104 extracted from

Heja, D.; Harmat, V.; Fodor, K.; Wilmanns, M.; Dobo, J.; Kekesi, K.A.; Zavodszky, P.; Gal, P.; Pal, G.
Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 are essential for lectin pathway activation and reveal structural plasticity of MASP-2 (2012), J. Biol. Chem., 287, 20290-20300.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Strucutre reveals significant plasticity of the protease	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY	randomization of positions P4, P2, P1, P1', P2', and P4' of the protease binding loop while keeping the structurally indispensable Cys at P3 and P3' leads to monospecific MASP inhibitors. Inhibitor variant FCTRKLCY is specific for isoform MASP-1	Homo sapiens
Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN	randomization of positions P4, P2, P1, P1', P2', and P4' of the protease binding loop while keeping the structurally indispensable Cys at P3 and P3' leads to monospecific MASP inhibitors. MASP-2 inhibitor variant VCTKLWCN completely blocks the lectin pathway activation	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00187	-	-

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000006	-	Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN	pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.058	-	Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY	pH not specified in the publication, temperature not specified in the publication	Homo sapiens

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Release 2023.1 (January 2023)