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TitleDissecting the Structure, Thermodynamic Stability, and Aggregation Properties of the A25T Transthyretin (A25T-TTR) Variant Involved in Leptomeningeal Amyloidosis: Identifying Protein Partners That Co-Aggregate during A25T-TTR Fibrillogenesis in Cerebrospinal Fluid.
Journal, issue, pagesBiochemistry, Vol. 50, Page 11070-11083, Year 2011
Publish dateAug 15, 2011 (structure data deposition date)
AuthorsAzevedo, E.P. / Pereira, H.M. / Garratt, R.C. / Kelly, J.W. / Foguel, D. / Palhano, F.L.
External linksBiochemistry / PubMed:22091638
MethodsX-ray diffraction
Resolution2.033 Å
Structure data

PDB-3tfb:
Transthyretin natural mutant A25T
Method: X-RAY DIFFRACTION / Resolution: 2.033 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHORMONE BINDING PROTEIN / Transthyretin / Immunoglobulin-like / Transport Protein / extracellular / HORMONE-BINDING PROTEIN

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