3BP5

Crystal structure of the mouse PD-1 and PD-L2 complex

3BP5 の概要

• エントリーDOI: 10.2210/pdb3bp5/pdb
• 関連するPDBエントリー: 3BP6
• 分子名称: Programmed cell death protein 1, Programmed cell death 1 ligand 2, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: pd-1, pd-l2, complex, costimulation, glycoprotein, immunoglobulin domain, membrane, transmembrane, receptor, signaling protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q02242; Cell membrane ; Single-pass type I membrane protein : Q9WUL5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36065.95

構造登録者

Yan, Q.,Lazar-Molnar, E.,Cao, E.,Ramagopal, U.A.,Toro, R.,Nathenson, S.G.,Almo, S.C. (登録日: 2007-12-18, 公開日: 2008-07-15, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)