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Structure paper

TitleToward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies.
Journal, issue, pagesJ. Med. Chem., Vol. 51, Page 6348-6358, Year 2008
Publish dateMar 24, 2008 (structure data deposition date)
AuthorsJohnson, S.M. / Connelly, S. / Wilson, I.A. / Kelly, J.W.
External linksJ. Med. Chem. / PubMed:18811132
MethodsX-ray diffraction
Resolution1.4 - 1.8 Å
Structure data

PDB-3cn0:
Human transthyretin (TTR) in complex with 3,5-Dimethyl-4-hydroxystilbene
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-3cn1:
Human transthyretin (TTR) in complex with 3,5-Dibromo-4-hydroxystilbene
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-3cn2:
Human transthyretin (TTR) in complex with 3,5-Dibromo-4-hydroxybiphenyl
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-3cn3:
Human transthyretin (TTR) in complex with 1,3-Dibromo-2-hydroxy-5-phenoxybenzene
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3cn4:
Human transthyretin (TTR) in complex with N-(3,5-Dibromo-4-hydroxyphenyl)benzamide
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-LJ1:
2,6-dimethyl-4-[(E)-2-phenylethenyl]phenol

ChemComp-HOH:
WATER

ChemComp-LJ2:
2,6-dibromo-4-[(E)-2-phenylethenyl]phenol

ChemComp-LJ3:
3,5-dibromobiphenyl-4-ol

ChemComp-LJ4:
2,6-dibromo-4-phenoxyphenol

ChemComp-LJ5:
N-(3,5-dibromo-4-hydroxyphenyl)benzamide

Source
  • homo sapiens (human)
KeywordsHormone / Transport protein / Transthyretin / Tetramer / Amyloid / Disease mutation / Gamma-carboxyglutamic acid / Glycoprotein / Polymorphism / Polyneuropathy / Retinol-binding / Secreted / Thyroid hormone / Transport / Vitamin A

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