efmarodocokin alfa   Click here for help

GtoPdb Ligand ID: 12212

Synonyms: IL-22Fc | RG 7880 | RG7880 | UTTR1147A
Compound class: Antibody
Comment: Efmarodocokin alfa is a recombinant human IL-22-Fc IgG4 fusion protein that acts as an agonist of the heterodimeric Interleukin-22α1/10β receptor which is expressed by epithelial cells. It activates the IL-22 signaling pathway without inducing systemic inflammation or causing immunosuppression. Efmarodocokin alfa was developed for potential to treat infectious or inflammatory diseases [2]. The most advanced investigation of its clinical utility has been of its potential to induce repair of the intestinal epithelial damage that is caused by inflammatory bowel diseases [1].
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Ligand Activity Visualisation Charts

These are box plot that provide a unique visualisation, summarising all the activity data for a ligand taken from ChEMBL and GtoPdb across multiple targets and species. Click on a plot to see the median, interquartile range, low and high data points. A value of zero indicates that no data are available. A separate chart is created for each target, and where possible the algorithm tries to merge ChEMBL and GtoPdb targets by matching them on name and UniProt accession, for each available species. However, please note that inconsistency in naming of targets may lead to data for the same target being reported across multiple charts.

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View interactive charts of activity data across species
Peptide Sequence Click here for help
APISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQP
YMQEVVPFLARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACIRVESKYGPPCPPCP
APEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFGSTYRVVSVLTVLH
QDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN
YKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK
Chemical Modification
The first 146 amino acids are human IL-22, with the remainder constituting the IgG4 Fc chain. There are 4 N-linked glycosylation sites in the IL-22 portion of the peptide, and the Fc region is fucosylated. Structurally efmarodocokin alfa is a dimer of the peptide shown. It has intramolecular disulfide bridges, and intermolecular disulfide bridges that link the subunits. The terminal lysine (K) residue from each chain is clipped.