What does this research mean for the field?

LTα binds to TNFR2 with lower affinity than TNFα, sharing a comparable overall receptor/ligand organization but differing in specific interface-stabilizing residues, including interactions involving the N-terminal region of LTα. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To determine the binding affinity, structural architecture, and residue-level interface contacts governing the interaction between tumor necrosis factor receptor 2 (TNFR2) and lymphotoxin α (LTα).

September 8, 2026Scientific ReportsOpen Access

Structural insights into the TNFR2/LTα interaction through an integrated experimental and computational approach

View Full Paper

Ask AI

Bookmark

Authors

GCGabriela Całka-KucUniversity of Gdańsk PSPaulina Stencel ABAngelika Becht

Discussion

Member takes

Implication

In vitro and computational study reveals the binding architecture and interface of the TNFR2/LTα complex, highlighting contact residues distinct from TNFα recognition.

Key Points

To determine the binding affinity, structural architecture, and residue-level interface contacts governing the interaction between tumor necrosis factor receptor 2 (TNFR2) and lymphotoxin α (LTα).
Measured binding affinities of mammalian- and bacterially expressed LTα for TNFR2 using spectral shift assays.
Mapped binding fragments using SPOT peptide synthesis and dot blot analysis to identify interactive sequences, particularly within the unresolved N-terminal region of LTα.
Constructed 1:3 and extended 3:3 TNFR2/LTα structural models and evaluated interface energetics using molecular dynamics simulations combined with MM-GBSA calculations.
Identified TNFR2-reactive peptides within the flexible N-terminal segment of LTα, allowing generation of an extended 3:3 complex model with partial agreement between experimental and predicted contacts.
Found that LTα and TNFα engage TNFR2 with comparable overall complex organization, but TNFα binds with substantially higher affinity.
Demonstrated that distinct residue-level energetic interactions stabilize the TNFR2/LTα interface compared to the TNFR2/TNFα complex.

Cite This Study

Całka-Kuc et al. (2026) studied this question.

synapsesocial.com/papers/6a9fd82f58e84d0ff5b47895 https://doi.org/10.1038/s41598-026-69890-9

View Full Paper

Ask AI

Bookmark

September 8, 2026Scientific ReportsOpen Access

Structural insights into the TNFR2/LTα interaction through an integrated experimental and computational approach

View Full Paper

Ask AI

Bookmark

Authors

GCGabriela Całka-KucUniversity of Gdańsk PSPaulina Stencel ABAngelika Becht

Discussion

Member takes

Implication

In vitro and computational study reveals the binding architecture and interface of the TNFR2/LTα complex, highlighting contact residues distinct from TNFα recognition.

Key Points

To determine the binding affinity, structural architecture, and residue-level interface contacts governing the interaction between tumor necrosis factor receptor 2 (TNFR2) and lymphotoxin α (LTα).
Measured binding affinities of mammalian- and bacterially expressed LTα for TNFR2 using spectral shift assays.
Mapped binding fragments using SPOT peptide synthesis and dot blot analysis to identify interactive sequences, particularly within the unresolved N-terminal region of LTα.
Constructed 1:3 and extended 3:3 TNFR2/LTα structural models and evaluated interface energetics using molecular dynamics simulations combined with MM-GBSA calculations.
Identified TNFR2-reactive peptides within the flexible N-terminal segment of LTα, allowing generation of an extended 3:3 complex model with partial agreement between experimental and predicted contacts.
Found that LTα and TNFα engage TNFR2 with comparable overall complex organization, but TNFα binds with substantially higher affinity.
Demonstrated that distinct residue-level energetic interactions stabilize the TNFR2/LTα interface compared to the TNFR2/TNFα complex.

Cite This Study

Całka-Kuc et al. (2026) studied this question.

synapsesocial.com/papers/6a9fd82f58e84d0ff5b47895 https://doi.org/10.1038/s41598-026-69890-9

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark