Structural and functional analysis of the costimulatory receptor programmed death-1

Xuewu Zhang, Jean Claude D. Schwartz, Xiaoling Guo, Sumeena Bhatia, Erhu Cao, Lieping Chen, Zhong Yin Zhang, Michael A. Edidin, Stanley G. Nathenson, Steven C. Almo

Research output: Contribution to journalArticle

202 Scopus citations


PD-1, a member of the CD28/CTLA-4/ICOS costimulatory receptor family, delivers negative signals that have profound effects on T and B cell immunity. The 2.0 Å crystal structure of the extracellular domain of murine PD-1 reveals an Ig V-type topology with overall similarity to the CTLA-4 monomer; however, there are notable differences in regions relevant to function. Our structural and biophysical data show that PD-1 is monomeric both in solution as well as on cell surface, in contrast to CTLA-4 and other family members that are all disulfide-linked homodimers. Furthermore, our structure-based mutagenesis studies identify the ligand binding surface of PD-1, which displays significant differences compared to those present in the other members of the family.

Original languageEnglish (US)
Pages (from-to)337-347
Number of pages11
Issue number3
StatePublished - Mar 1 2004


ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

Cite this

Zhang, X., Schwartz, J. C. D., Guo, X., Bhatia, S., Cao, E., Chen, L., Zhang, Z. Y., Edidin, M. A., Nathenson, S. G., & Almo, S. C. (2004). Structural and functional analysis of the costimulatory receptor programmed death-1. Immunity, 20(3), 337-347.