| First Author | Zhang X | Year | 2004 |
| Journal | Immunity | Volume | 20 |
| Issue | 3 | Pages | 337-47 |
| PubMed ID | 15030777 | Mgi Jnum | J:89777 |
| Mgi Id | MGI:3041387 | Doi | 10.1016/s1074-7613(04)00051-2 |
| Citation | Zhang X, et al. (2004) Structural and functional analysis of the costimulatory receptor programmed death-1. Immunity 20(3):337-47 |
| abstractText | 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. |
