Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure-guided engineering of CD112 receptor variants for optimized immunotherapy.

Molecular therapy : the journal of the American Society of Gene Therapy - 6 Aug 2025

Singh Srishti, Julia Estefania, Kalita Parismita, Mason Charlotte, Ming Qianqian, Lee-Sam Ansar, Gordon Sumai, Buitrago Maria Emilia, Leung Daisy W, Hwu Patrick, Luca Vincent C

Abstract excerpt

The immune checkpoint protein, CD112 receptor (CD112R, also known as PVRIG), suppresses T and natural killer (NK) cell activation upon binding to tumor-expressed CD112 (Nectin-2) ligands. Here, we determine the structure of the CD112-CD112R complex and use it to guide the engineering of multiple CD112-targeting immunotherapy candidates. The 2.2 Å-resolution crystal structure reveals an antiparallel, lock-and-key...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Line, Tumor
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunotherapy

Share to Lymphocyte Activation

Share to Protein Engineering

Share to Protein Multimerization

Share to Receptors, Chimeric Antigen

Share to T-Lymphocytes

Source

Open in PubMed Open full text

Identifiers

PMID: 40285356
DOI: 10.1016/j.ymthe.2025.04.032
PMCID: PMC12368799

Genes

PVRIG

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-guided engineering of CD112 receptor variants for optimized immunotherapy.PMID 40285356Read ↗

Engineering NKG2D ligand affinity transforms EGFR-targeted NK cell engagers into high-potency effectors against pancreatic cancerSemantic proximity Read ↗

Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2.Semantic proximity Read ↗

Insights into the binding recognition and computational design of IL-2 muteins with enhanced predicted binding affinity to the IL-2 receptor α.Semantic proximity Read ↗

Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies.Semantic proximity Read ↗

A high-affinity human PD-1/PD-L2 complex informs avenues for small-molecule immune checkpoint drug discoverySemantic proximity Read ↗

Affinity maturation, humanization, and co-crystallization of a rabbit anti-human ROR2 monoclonal antibody for therapeutic applicationsSemantic proximity Read ↗

Computer-aided design of PVR mutants with enhanced binding affinity to TIGIT.Semantic proximity Read ↗

Structure and Functional Binding Epitope of V-domain Ig Suppressor of T Cell ActivationSemantic proximity Read ↗

Directed disruption of IL2 aggregation sites produces designer biologics with enhanced specificity coupled to improved production capacitySemantic proximity Read ↗

Characterizing the regulatory Fas (CD95) epitope critical for agonist antibody targeting and CAR-T bystander function in ovarian cancerSemantic proximity Read ↗

A broad matrix metalloproteinase inhibitor with designed loop extension exhibits ultrahigh specificity for MMP-14Semantic proximity Read ↗

Human and viral membrane-associated E3 ubiquitin ligases MARCH1 and MIR2 recognize different features of CD86 to downregulate surface expression.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.