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TitleIodination of salicylic acid improves its binding to transthyretin
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1784, Page 512-517, Year 2008
Publish dateOct 25, 2007 (structure data deposition date)
AuthorsGales, L. / Almeida, M.R. / Arsequell, G. / Valencia, G. / Saraiva, M.J. / Damas, A.M.
External linksBiochim. Biophys. Acta / PubMed:18155178
MethodsX-ray diffraction
Resolution1.55 Å
Structure data

PDB-3b56:
Crystal structure of transthyretin in complex with 3,5-diiodosalicylic acid
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-DIU:
2-HYDROXY-3,5-DIIODO-BENZOIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / TRANSTHYRETIN / AMYLOID INHIBITORS / IODINE / Disease mutation / Glycoprotein / Hormone / Polymorphism / Polyneuropathy / Retinol-binding / Secreted / Thyroid hormone / Transport / Vitamin A

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