3bp5
From Proteopedia
Crystal structure of the mouse PD-1 and PD-L2 complex
Structural highlights
Function[PDCD1_MOUSE] Inhibitory cell surface receptor involved in the regulation of T-cell function during immunity and tolerance. Upon ligand binding, inhibits T-cell effector functions in an antigen-specific manner. Possible cell death inducer, in association with other factors (By similarity). [PD1L2_MOUSE] Involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProgrammed 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. Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2.,Lazar-Molnar E, Yan Q, Cao E, Ramagopal U, Nathenson SG, Almo SC Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10483-8. Epub 2008 Jul 18. PMID:18641123[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Mus musculus | Almo, S C | Cao, E | Lazar-Molnar, E | Nathenson, S G | Ramagopal, U A | Toro, R | Yan, Q | Complex | Costimulation | Glycoprotein | Immunoglobulin domain | Membrane | Pd-1 | Pd-l2 | Receptor | Signaling protein | Transmembrane
