1NPU

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE PD-1

Summary for 1NPU

• Entry DOI: 10.2210/pdb1npu/pdb
• Related: 1B88
• Descriptor: Programmed cell death protein 1 (2 entities in total)
• Functional Keywords: ig v-type domain, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, immune system
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 13176.71

Authors

Zhang, X.,Schwartz, J.-C.D.,Guo, X.,Cao, E.,Chen, L.,Zhang, Z.-Y.,Nathenson, S.G.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-01-20, release date: 2004-03-23, Last modification date: 2024-10-30)

Primary citation

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

PubMed 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.

PubMed: 15030777
DOI: 10.1016/S1074-7613(04)00051-2

Experimental method

X-RAY DIFFRACTION (2 Å)