Literature summary for 3.4.21.107 extracted from

Ciferri, C.; Lipari, M.T.; Liang, W.C.; Estevez, A.; Hang, J.; Stawicki, S.; Wu, Y.; Moran, P.; Elliott, M.; Eigenbrot, C.; Katschke, K.J.; van Lookeren Campagne, M.; Kirchhofer, D.
The trimeric serine protease HtrA1 forms a cage-like inhibition complex with an anti-HtrA1 antibody (2015), Biochem. J., 472, 169-181 .

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Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9R118	-	-

Synonyms

Synonyms	Comment	Organism
HtrA1	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	antibody 94,obtained from a human antibody phage display library, forms a distinct macromolecular complex with HtrA1 and inhibits the enzymatic activity of recombinant and native HtrA1 forms. The 246-kDa complex between the HtrA1 catalytic domain trimer and Fab94 has a propeller-like organization with one Fab bound peripherally to each protomer. The antibody binds to the surface-exposed loops B and C of the catalytic domain. The the HtrA1 catalytic domain-IgG94 complex (636 kDa) is a cage-like structure with three centrally located IgG94 molecules coordinating two the HtrA1 catalytic domain trimers and the six active sites pointing into the cavity of the cage. In both complexes, all antigen-recognition regions bind one HtrA1 protomer and all protomers are bound by a antigen-recognition region	Mus musculus

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Release 2023.1 (January 2023)