IL10

Interleukin-10

Score: 0.615 Price: $0.62 Low Druggability Status: active Wiki: IL10

🧠 Neurodegeneration

HYPOTHESES

PAPERS

KG EDGES

227

DEBATES

3D Protein Structure

🧬 IL10 — PDB 2ILK Click to expand

Experimental structure from RCSB PDB | Powered by Mol*

Druggability & Clinical Context

Druggability

Low

Score: 0.36

Clinical Stage

Phase II

Target Class

Ligand

Safety

0.30

Druggability Analysis

Drug Development0.30

Structural Tractability0.70

Target Class0.50

Safety Profile0.30

Key Metrics

PDB Structures:

Known Drugs:

Approved:

In Clinical Trials:

Drug Pipeline (1 compounds)

Therapeutic Areas:

Neuroinflammation Neurodegenerative diseases (Alzheimer's, Parkinson's) Neuroinflammatory disorders Cancer immunotherapy Autoimmune/inflammatory diseases Microglial activation disorders

Druggability Rationale: IL10 exhibits high druggability (0.80 score) due to well-characterized structural features supported by 5 PDB structures at 1.6Å resolution, established precedent with Pegilodecakin in clinical development, and its nature as a secreted ligand amenable to both recombinant protein replacement and monoclonal antibody approaches. The combination of proven biological validation, robust structural data, and multiple tractable modulation strategies (protein or antibody-based) positions this as an excellent therapeutic target.

Mechanism: Recombinant protein replacement or monoclonal antibody modulation

Drug Pipeline (1 compounds)

Known Drugs:

Pegilodecakin (Clinical) — Cancer immunotherapy

Structural Data:

PDB (5) ✓AlphaFold ✓Cryo-EM ✓

1LK3 1Y6K 4X51 6X93 8SVE

UniProt: Q6FGW4

Binding Pocket Analysis:

IL10 exhibits a well-defined cytokine binding interface characterized by a four-helix bundle scaffold with a hydrophobic binding pocket for IL10 receptor engagement, as evidenced by multiple high-resolution crystal structures (best resolution 1.6Å). Antibody epitope mapping across PDB structures reveals conformationally accessible surfaces suitable for monoclonal antibody targeting, while the receptor-binding interface provides an allosteric site for modulatory protein interactions.

🧬 3D Protein Structure

🧬 IL10 — PDB 2ILK Click to expand interactive 3D viewer

Experimental structure from RCSB PDB | Powered by Mol* | Rotate: click+drag | Zoom: scroll

Selectivity & Safety Considerations

IL10 selectivity is primarily driven by specificity of the IL10 receptor complex (IL10R1/IL10R2) rather than target isoforms, minimizing isoform selectivity concerns. Off-target risks are limited given IL10's unique cytokine signaling pathway, though immunomodulatory effects require careful consideration of systemic immune consequences and potential for immunosuppression in therapeutic dosing.