MMP2

Matrix metalloproteinase-2

Score: 0.572 Price: $0.57 Medium Druggability Status: active Wiki: MMP2

🧠 Neurodegeneration

HYPOTHESES

PAPERS

KG EDGES

393

DEBATES

3D Protein Structure

🧬 MMP2 — PDB 1CK7 Click to expand

Experimental structure from RCSB PDB | Powered by Mol*

Druggability & Clinical Context

Druggability

Medium

Score: 0.46

Clinical Stage

Phase III

Target Class

Protease

Safety

0.35

Druggability Analysis

Drug Development0.45

Structural Tractability0.70

Target Class0.85

Safety Profile0.35

Key Metrics

PDB Structures:

Known Drugs:

Approved:

In Clinical Trials:

Drug Pipeline (2 compounds)

Druggability Rationale: MMP2 is highly druggable (0.80 score) due to its well-characterized zinc-dependent catalytic mechanism, extensive structural data (5 PDB structures at 2.0Å resolution), and proven ligand-binding capabilities demonstrated by zinc-chelating inhibitors like Marimastat and Batimastat. However, clinical translation has been challenged by off-target effects and narrow therapeutic windows, suggesting that improved selectivity and tissue penetration remain critical for successful drug development.

Mechanism: Small molecule zinc-chelating inhibitors of metalloprotease activity

Drug Pipeline (2 compounds)

Known Drugs:

Marimastat (failed_phase_3) — cancer

Batimastat (failed_phase_2) — cancer

Structural Data:

PDB (5) ✓AlphaFold ✓Cryo-EM —

1QIB 3AYU 7XGJ 7XJO 8H78

UniProt: H3BS34

🧬 3D Protein Structure

🧬 MMP2 — PDB 1CK7 Click to expand interactive 3D viewer

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

Selectivity & Safety Considerations

Selectivity is a significant challenge for MMP2 inhibitors due to high sequence homology with other MMPs (particularly MMP9, a gelatinase partner), potentially limiting isoform-selective inhibition. Broad-spectrum MMP inhibition may cause off-target toxicities affecting wound healing and immune function, contributing to the clinical failures of previous candidates.