Structural Modeling Assessment of CCR5–PD-L1–bNAb Triplet Geometry

This dataset accompanies the structural modeling report “Structural Modeling Update: Triplet-Axis Assembly” (FireGate Biotech Inc.). The work evaluates whether CCR5 antagonism, PD-L1 modulation, and PD-L1-directed antibody activity could plausibly operate through a single three-body structural complex. Curated Protein Data Bank structures for CCR5 (4MBS), PD-L1 (8GAD), and a PD-L1-targeted nanobody used as an antibody proxy (5DXW) were opened and examined in UCSF ChimeraX (daily build, 2025-10-13, macOS). Models were aligned, colored, and inspected for steric compatibility, using an approximate clash threshold of 4 Å. In all explored orientations, no sterically permissive triplet geometry was identified, suggesting that synergy across these axes is more likely mediated by indirect regulatory and signaling interactions rather than direct CCR5–PD-L1–antibody co-binding. The figures and any included ChimeraX sessions are intended to document this conceptual geometric assessment. They are not clinical data and do not represent validated therapeutic outcomes.