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Structural insight into T cell coinhibition by PD-1H (VISTA). | LitMetric

Structural insight into T cell coinhibition by PD-1H (VISTA).

Proc Natl Acad Sci U S A

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520

Published: January 2020

AI Article Synopsis

Article Abstract

Programmed death-1 homolog (PD-1H), a CD28/B7 family molecule, coinhibits T cell activation and is an attractive immunotherapeutic target for cancer and inflammatory diseases. The molecular basis of its function, however, is unknown. Bioinformatic analyses indicated that PD-1H has a very long Ig variable region (IgV)-like domain and extraordinarily high histidine content, suggesting that unique structural features may contribute to coinhibitory mechanisms. Here we present the 1.9-Å crystal structure of the human PD-1H extracellular domain. It reveals an elongated CC' loop and a striking concentration of histidine residues, located in the complementarity-determining region-like proximal half of the molecule. We show that surface-exposed histidine clusters are essential for robust inhibition of T cell activation. PD-1H exhibits a noncanonical IgV-like topology including an extra "H" β-strand and "clamping" disulfide, absent in known IgV-like structures, that likely restricts its orientation on the cell surface differently from other IgV-like domains. These results provide important insight into a molecular basis of T cell coinhibition by PD-1H.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6983362PMC
http://dx.doi.org/10.1073/pnas.1908711117DOI Listing

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