3BOV

Crystal structure of the receptor binding domain of mouse PD-L2

Summary for 3BOV

• Entry DOI: 10.2210/pdb3bov/pdb
• Descriptor: Programmed cell death 1 ligand 2, SODIUM ION, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: pd-l2; b7-dc, programmed death-1 ligand2, glycoprotein, immunoglobulin domain, membrane, receptor, transmembrane, immune system
• Biological source: Mus musculus (Mouse)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q9WUL5
• Total number of polymer chains: 1
• Total formula weight: 11891.46

Authors

Lazar-Molnar, E.,Ramagopal, U.,Cao, E.,Toro, R.,Nathenson, S.G.,Almo, S.C. (deposition date: 2007-12-17, release date: 2008-07-15, Last modification date: 2024-11-13)

Primary citation

Lazar-Molnar, E.,Yan, Q.,Cao, E.,Ramagopal, U.,Nathenson, S.G.,Almo, S.C.
Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2.
Proc.Natl.Acad.Sci.USA, 105:10483-10488, 2008

PubMed Abstract: Programmed death-1 (PD-1) is a member of the CD28/B7 superfamily that delivers negative signals upon interaction with its two ligands, PD-L1 or PD-L2. The high-resolution crystal structure of the complex formed by the complete ectodomains of murine PD-1 and PD-L2 revealed a 1:1 receptor:ligand stoichiometry and displayed a binding interface and overall molecular organization distinct from that observed in the CTLA-4/B7 inhibitory complexes. Furthermore, our structure also provides insights into the association between PD-1 and PD-L1 and highlights differences in the interfaces formed by the two PD-1 ligands (PD-Ls) Mutagenesis studies confirmed the details of the proposed PD-1/PD-L binding interfaces and allowed for the design of a mutant PD-1 receptor with enhanced affinity. These studies define spatial and organizational constraints that control the localization and signaling of PD-1/PD-L complexes within the immunological synapse and provide a basis for manipulating the PD-1 pathways for immunotherapy.

PubMed: 18641123
DOI: 10.1073/pnas.0804453105

Experimental method

X-RAY DIFFRACTION (1.77 Å)