Crystallography in Action: Understanding Adalimumab

Modern medicines such as adalimumab (pictured above)—a monoclonal antibody used to treat rheumatoid arthritis, Crohn's disease, psoriasis, and other autoimmune disorders—are made possible by our ability to understand biological structures at the atomic level.

Adalimumab works by binding to tumor necrosis factor-alpha (TNF-α), a protein that plays a central role in inflammation. Determining the three-dimensional structures of antibodies, TNF-α, and the complexes they form has been made possible through crystallographic techniques. By revealing how these molecules interact, crystallography provides the structural insights needed to develop therapies that can precisely target disease-causing pathways while minimizing effects on healthy tissues.

 Crystallographic Data 
The molecular structure shown here is based on crystallographic studies of adalimumab's antigen-binding region (Fab fragment), which have revealed how the antibody recognizes its target at the atomic level. We acknowledge and thank the scientists who contributed these structural data to the Protein Data Bank (PDB), an essential global archive that supports research, education, and innovation in structural science.

PDB ID: 4NYL (Adalimumab Fab fragment)

PDB ID: 3WD5 (Adalimumab Fab complexed with human TNF\(\alpha \))

 

Today, structural biology and crystallography remain essential tools in the discovery and improvement of biopharmaceuticals. From understanding protein function to guiding the design of next-generation therapeutics, crystallography continues to transform medicine and improve lives around the world.

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