PD-1H/VISTA: Crystal Structure of Human Immune Checkpoint Protein

A 1.9-Å crystal structure reveals the unique elongated CC' loop and histidine clusters of the human PD-1H extracellular domain. The structure, determined by researchers at Yale University, exhibits a noncanonical IgV-like topology with an extra 'H' β-strand and a 'clamping' disulfide. These features provide molecular insight into how PD-1H coinhibits T cell activation, a mechanism relevant for cancer and inflammatory disease therapies.

Use Cases

• Analyzing protein-protein interaction interfaces based on the described surface-exposed histidine clusters.
• Studying structural variations in IgV-like domains based on the described noncanonical topology.
• Designing immunotherapeutic drugs targeting PD-1H based on the detailed atomic coordinates.
• Investigating the role of disulfide bonds in protein stability based on the described 'clamping' disulfide.

Strengths

• High-resolution 1.9-Å crystal structure provides detailed atomic coordinates.
• Structure reveals specific, unique features like an elongated CC' loop and a high concentration of histidine residues.
• Analysis links structural features (histidine clusters) to functional outcomes (inhibition of T cell activation).

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Data may reflect the specific experimental and crystallographic bias inherent to paperswithcode.

Provenance

Source

Yale University

Collection Method

X-ray crystallography