SQT-1C: Engineered Protein Scaffold Crystal Structure and Oligomerization Data

C.W. Levy from the University of Manchester presents structural data on the engineered protein scaffold SQT-1C. The dataset includes the X-ray crystal structure revealing a cystatin-like fold and analysis of its oligomerization into dimers and tetramers in solution, studied via NMR and molecular dynamics simulations. The work investigates the structural consequences of peptide insertions on scaffold stability and solution behavior.

Use Cases

• Modeling protein oligomerization mechanisms based on the described domain-swap and interface-symmetry findings.
• Assessing scaffold stability after peptide insertion based on the structural and solution behavior data.
• Training models to predict 3D structural changes from retained secondary structure using the described case study.
• Designing protein-protein interaction interfaces based on the analysis of inserted loops comprising the oligomer interface.

Strengths

• Structural data derived from X-ray crystallography provides atomic-level detail.
• Solution behavior characterized using multiple complementary methods (NMR, molecular dynamics).
• Analysis compares two specific oligomerization mechanisms with thermodynamic assessment.

Limitations

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

Provenance

Source

University of Manchester

Collection Method

Experimental structural biology (X-ray crystallography, NMR) and computational simulations (molecular dynamics).