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Literature summary for 3.4.21.79 extracted from
- Design and characterization of a novel human granzyme B inhibitor (2015), Protein Eng. Des. Sel., 28, 9-17 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| engineered chimeric human antichymotrypsin | engineering of a extracellular GrB serpin: a chimeric protein is generated in which the reactive center loop (RCL) of human extracellular antichymotrypsin (ACT) is replaced with that of serpina3n, a mouse extracellular inhibitor of GrB lacking in humans. This serpin contains 27 amino acid residues from the serpina3n RCL and the remaining 395 residues from human ACT. The insertion converts human ACT into a GrB-inhibitory serpin. Several critical residues are identified by scanning mutagenesis on the chimera and serpina3n. Targeted mutagenesis is conducted on wild-type human ACT by specifically substituting those critical residues, creating an inhibitor that contains 99.3% human ACT sequence with only three point mutations. Inhibition kinetics | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P10144 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GrB | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | intracellular role of Granzyme B (GrB) in immune-mediated cell killing. Enzyme GrB is also implicated in extracellular pathways of inflammation, cytokine activation and autoimmunity | Homo sapiens |
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Release 2023.1 (January 2023)
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