Literature summary for 3.4.21.20 extracted from

de Garavilla, L.; Greco, M.N.; Sukumar, N.; Chen, Z.W.; Pineda, A.O.; Mathews, F.S.; Di Cera, E.; Giardino, E.C.; Wells, G.I.; Haertlein, B.J.; Kauffman, J.A.; Corcoran, T.W.; Derian, C.K.; Eckardt, A.J.; Damiano, B.P.; Andrade-Gordon, P.; Maryanoff, B.E.
A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo (2005), J. Biol. Chem., 280, 18001-18007.

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Application

Application	Comment	Organism
medicine	JNJ-10311795 is an inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an exciting opportunity in the treatment of asthma and chronic obstructive pulmonary disease	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme complexed with the inhibitor JNJ-10311795, 1.85 A resolution	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
JNJ-10311795	inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an opportunity in the treatment of asthma and chronic obstructive pulmonary disease	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P08311	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
neutrophil	-	Homo sapiens	-

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000038	-	JNJ-10311795	-	Homo sapiens

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Release 2023.1 (January 2023)