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TitleCavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation.
Journal, issue, pagesSci Rep, Vol. 7, Page 44709-44709, Year 2017
Publish dateNov 17, 2015 (structure data deposition date)
AuthorsSant'Anna, R. / Almeida, M.R. / Varejao, N. / Gallego, P. / Esperante, S. / Ferreira, P. / Pereira-Henriques, A. / Palhano, F.L. / de Carvalho, M. / Foguel, D. ...Sant'Anna, R. / Almeida, M.R. / Varejao, N. / Gallego, P. / Esperante, S. / Ferreira, P. / Pereira-Henriques, A. / Palhano, F.L. / de Carvalho, M. / Foguel, D. / Reverter, D. / Saraiva, M.J. / Ventura, S.
External linksSci Rep / PubMed:28338000
MethodsX-ray diffraction
Resolution1.3 - 1.449 Å
Structure data

PDB-5fo2:
Structure of human transthyretin mutant A108I
Method: X-RAY DIFFRACTION / Resolution: 1.449 Å

PDB-5fw6:
Structure of human transthyretin mutant A108V
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / T4-BINDING PROTEIN NON-AMYLOIDOGENIC / TRASNPORT PROTEIN / T4-BINDING

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