Crystal Structure of the Human TLR2-Diprovocim Complex

A crystal structure reveals the binding mode of Diprovocim, a synthetic small molecule agonist, to the human Toll-like receptor 2 (TLR2) ectodomain. The structure shows two Diprovocim molecules bound in a ligand pocket formed between two TLR2 ectodomains, with extensive hydrophobic interactions and a hydrogen-bonding network. This work by Haiyang Zhang provides the first structural insight into TLR2/TLR1 activation by a noncanonical agonist.

Use Cases

• Analyzing protein-ligand interactions based on the described hydrophobic and hydrogen-bonding network.
• Studying TLR2 dimerization mechanisms based on the observed TLR2 homodimer and heterodimer formation.
• Informing structure-based drug design for TLR2/TLR1 agonists based on the defined ligand binding pocket.

Strengths

• The dataset is derived from a determined crystal structure, providing atomic-level detail.
• The description details specific molecular interactions, such as hydrophobic contacts and a hydrogen-bonding network.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Haiyang Zhang via paperswithcode

Collection Method

Determined through in vitro biophysical, structural, and computational approaches as described.