Protein-protein interface in immune signaling

Protein-protein interfaces in immune signaling are the physical contact surfaces formed between immune-related proteins (notably cell surface receptors, ligands, and adapter molecules) that underpin the dynamic regulation of immune cell communication, activation, and suppression. These interfaces mediate critical events such as antigen recognition, costimulation, checkpoint control, and cytokine signaling. Disruption or modulation of these interfaces has yielded potent immunotherapies (notably immune checkpoint blockade), but also brings challenges regarding specificity, toxicity, and resistance. The structural characterization of these interfaces is a vibrant field for therapeutic and diagnostic innovation, encompassing monoclonal antibodies, small molecules, and peptide therapeutics that modulate PPI networks central to immune function. The use of this name as a "target" is inherently broad and refers to a structurally and functionally heterogeneous set of molecular sites. For a drug or screening effort, this class must be reduced to specific protein pairs (e.g., PD-1/PD-L1, CD20/CD21, etc.) for actionable target-based applications.

Other names

protein-protein interfacesPPI sites in immune signalingimmune PPI interfacesimmune cell interactome interfaces

Inhibition or disruption of protein-protein interactions at critical surfaces (e.g., checkpoint blockade) Stabilization or mimicry of interface interactions Allosteric modulation of interface conformation