Structural and Functional Analysis of the Costimulatory Receptor Programmed Death-1

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• 作者：Xuewu Zhang ; Jean-Claude D. Schwartz ; Xiaoling Guo ; Sumeena Bhatia ; Erhu Cao ; Lieping Chen ; Zhong-Yin Zhang ; Michael A. Edidin ; Stanley G. Nathenson and Steven C. Almo
• 刊名：Immunity
• 出版年：2004
• 出版时间：March 2004
• 年：2004
• 卷：20
• 期：3
• 页码：337-347
• 全文大小：1127 K

文摘

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.