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Structure paper

TitleToward optimization of the second aryl substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies.
Journal, issue, pagesJ. Med. Chem., Vol. 52, Page 1115-1125, Year 2009
Publish dateOct 6, 2008 (structure data deposition date)
AuthorsJohnson, S.M. / Connelly, S. / Wilson, I.A. / Kelly, J.W.
External linksJ. Med. Chem. / PubMed:19191553
MethodsX-ray diffraction
Resolution1.31 - 1.35 Å
Structure data

PDB-3esn:
Human transthyretin (TTR) complexed with N-(3,5-Dibromo-4-hydroxyphenyl)-2,6-dimethylbenzamide
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-3eso:
Human transthyretin (TTR) complexed with N-(3,5-Dibromo-4-hydroxyphenyl)-2,5-dichlorobenzamide
Method: X-RAY DIFFRACTION / Resolution: 1.31 Å

PDB-3esp:
Human transthyretin (TTR) complexed with N-(3,5-Dibromo-4-hydroxyphenyl)-3,5-dimethyl-4-hydroxybenzamide
Method: X-RAY DIFFRACTION / Resolution: 1.31 Å

Chemicals

ChemComp-DZ1:
N-(3,5-dibromo-4-hydroxyphenyl)-2,6-dimethylbenzamide

ChemComp-HOH:
WATER

ChemComp-DZ2:
2,5-dichloro-N-(3,5-dibromo-4-hydroxyphenyl)benzamide

ChemComp-DZ3:
N-(3,5-dibromo-4-hydroxyphenyl)-4-hydroxy-3,5-dimethylbenzamide

Source
  • homo sapiens (human)
KeywordsHORMONE / Growth Factor / Amyloid / Disease mutation / Gamma-carboxyglutamic acid / Glycoprotein / Polymorphism / Polyneuropathy / Retinol-binding / Secreted / Thyroid hormone / Transport / Vitamin A

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