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TitleConformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding.
Journal, issue, pagesJ. Struct. Biol., Vol. 170, Page 522-531, Year 2010
Publish dateOct 29, 2009 (structure data deposition date)
AuthorsTrivella, D.B. / Bleicher, L. / Palmieri, L.C. / Wiggers, H.J. / Montanari, C.A. / Kelly, J.W. / Lima, L.M. / Foguel, D. / Polikarpov, I.
External linksJ. Struct. Biol. / PubMed:20211733
MethodsX-ray diffraction
Resolution1.8 - 1.95 Å
Structure data

PDB-3kgs:
V30M mutant human transthyretin (TTR) (apoV30M) pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3kgt:
V30M mutant human transthyretin (TTR) complexed with genistein (V30M:GEN) pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3kgu:
Wild type human transthyretin (TTR) complexed with genistein (TTRwt:GEN) pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GEN:
GENISTEIN

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / TTR / TRANSTHYRETIN / AMYLOID / Amyloidosis / Hormone / Neuropathy / Polymorphism / Secreted / Thyroid hormone / Transport / Cytoplasm / Disease mutation

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