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TitleRole of the Glutamic Acid 54 Residue in Transthyretin Stability and Thyroxine Binding
Journal, issue, pagesBiochemistry, Year 2009
Publish dateJul 6, 2009 (structure data deposition date)
AuthorsMiyata, M. / Sato, T. / Mizuguchi, M. / Nakamura, T. / Ikemizu, S. / Nabeshima, Y. / Susuki, S. / Suwa, Y. / Morioka, H. / Ando, Y. ...Miyata, M. / Sato, T. / Mizuguchi, M. / Nakamura, T. / Ikemizu, S. / Nabeshima, Y. / Susuki, S. / Suwa, Y. / Morioka, H. / Ando, Y. / Suico, M.A. / Shuto, T. / Koga, T. / Yamagata, Y. / Kai, H.
External linksBiochemistry / PubMed:19950966
MethodsX-ray diffraction
Resolution1.7 - 2 Å
Structure data

PDB-3a4d:
Crystal structure of Human Transthyretin (wild-type)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3a4e:
Crystal structure of Human Transthyretin (E54G)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3a4f:
Crystal Structure of Human Transthyretin (E54K)
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / BETA BARREL / Amyloid / Amyloidosis / Disease mutation / Gamma-carboxyglutamic acid / Glycoprotein / Hormone / Neuropathy / Retinol-binding / Secreted / Thyroid hormone / Transport / Vitamin A / THYROXINE

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