Human Transthyretin and Val-30-Met Variant X-Ray Crystal Structures at 1.7-A Resolution

X-ray crystal structure refinements for normal human transthyretin and the amyloidogenic Val-30-Met variant, refined to 1.7-A resolution. The dataset includes R-values and stereochemical parameter standard deviations for bond and angle distances. The structures were refined by B.C. Braden, with improvements over a prior 1971 structure.

Use Cases

• Modeling protein-ligand interactions based on the described thyroxine-binding cavity.
• Studying the structural impact of point mutations based on the Val-30-Met substitution.
• Comparing protein conformation and loop regions based on the refined normal structure.
• Analyzing beta-sheet distortions in monomers based on the described 1 A separation.

Strengths

• Structures refined to a high resolution of 1.7 angstroms.
• Includes specific R-values (0.168 and 0.179) and standard deviations for stereochemical parameters.
• Refinement resolved specific residues (Arg-103, Thr-123, Asn-124, Pro-125) and modeled terminal residues using simulated annealing.

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

B.C. Braden, Indiana University – Purdue University Indianapolis

Collection Method

X-ray crystallography refinement