What question did this study set out to answer?

The aim is to explore the binding mode of Factor VIIa and its potential for novel inhibition methods.

February 2, 2026ChemMedChem

Nonstandard Factor VIIa Binding Mode Reveals S1 Pocket Plasticity in Trypsin‐Like Proteases

View Full Paper

Ask AI

Bookmark

Authors

X-ray crystallography reveals S1 pocket plasticity in serine proteases, suggesting new FVIIa inhibition strategies.

The aim is to explore the binding mode of Factor VIIa and its potential for novel inhibition methods.
Utilized X-ray crystallography to analyze the FVIIa-tissue factor complex with a bound inhibitor.
Conducted 0.17 ms of atomistic molecular dynamics simulations on FVIIa and 12 other serine peptidases.
Investigated conformational transitions of the S1 pocket in various conditions.
Identified a remodeled active site and collapsed S1 pocket of FVIIa with inhibited state.
Demonstrated dynamic transitions between open and collapsed S1 pockets in FVIIa and 12 other serine proteases.
Highlighted the general plasticity of the S1 pocket, suggesting new inhibition pathways for FVIIa.

Tesmer et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark