(Journal Article): Structural and functional analysis of the costimulatory receptor programmed death-1.
 
Zhang X, Schwartz JC, Guo X, Bhatia S, Cao E, Lorenz M, Cammer M, Chen L, Zhang ZY, Edidin MA, Nathenson SG, Almo SC (Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461 USA.)
 
IN: Immunity 2004; 20(3):337-347
Impact Factor(s) of Immunity: 1.545 (2004), 16.016 (2003), 17.468 (2002), 18.866 (2001)

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ABSTRACT: 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 A 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.

TYPE OF PUBLICATION: Original article

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