PRMT1

Protein arginine methyltransferase 1

Score: 0.611 Price: $0.61 Low Druggability Status: active Wiki: PRMT1

🧠 Neurodegeneration

HYPOTHESES

PAPERS

KG EDGES

157

DEBATES

3D Protein Structure

🧬 PRMT1 — PDB 1OR8 Click to expand

Experimental structure from RCSB PDB | Powered by Mol*

Druggability & Clinical Context

Druggability

Low

Score: 0.36

Clinical Stage

Phase I

Target Class

Epigenetic Regulator

Safety

0.50

Druggability Analysis

Drug Development0.15

Structural Tractability0.70

Target Class0.70

Safety Profile0.50

Key Metrics

PDB Structures:

Known Drugs:

Approved:

In Clinical Trials:

Drug Pipeline (1 compounds)

Therapeutic Areas:

Neurodegeneration (Alzheimer's disease, Parkinson's disease) ALS (Amyotrophic lateral sclerosis) Frontotemporal dementia RNA processing disorders DNA repair deficiencies

Druggability Rationale: PRMT1 presents moderate druggability (0.55 score) supported by extensive structural data (9 PDB structures at 2.48 Å resolution) and a defined substrate binding pocket, though the target lacks approved drugs beyond tool compounds like MS023. The epigenetic regulator class is increasingly tractable, but achieving potency and selectivity against related PRMT family members remains challenging.

Mechanism: Small molecule inhibitor of protein arginine methyltransferase activity

Drug Pipeline (1 compounds)

Known Drugs:

MS023 (tool_compound) — research

Structural Data:

PDB (9) ✓AlphaFold ✓Cryo-EM ✓

3Q7E 6NT2 8Z2Z 8Z7H 8Z7O+4 more

UniProt: A0A3S6H7X9

Binding Pocket Analysis:

PRMT1 contains a conserved SAM (S-adenosylmethionine) cofactor binding pocket and a substrate arginine recognition site, as defined by high-resolution crystal structures (PDB: 3Q7E, 6NT2, 8Z2Z). The binding pocket accommodates both cofactor and protein substrate simultaneously, offering opportunities for dual-site or allosteric inhibition strategies.

🧬 3D Protein Structure

🧬 PRMT1 — PDB 1OR8 Click to expand interactive 3D viewer

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

Selectivity & Safety Considerations

PRMT1 selectivity is complicated by nine human PRMT family members (PRMT1-9) with overlapping substrate specificities and shared catalytic mechanisms. Off-target engagement with PRMT4/CARM1, PRMT6, and PRMT8 represents a significant risk requiring isoform-selective chemical design.