English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structure of monomeric transthyretin carrying the clinically important T119M mutation.

MPS-Authors
/persons/resource/persons195024

Oroz,  J.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

2407599_Suppl.pdf
(Supplementary material), 286KB

Citation

Kim, J. H., Oroz, J., & Zweckstetter, M. (2016). Structure of monomeric transthyretin carrying the clinically important T119M mutation. Angewandte Chemie International Edition, 55(52), 16168-16171. doi:10.1002/anie.201608516.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-A696-0
Abstract
Mutations in the protein transthyretin can cause as well as protect individuals from transthyretin amyloidosis, an incurable fatal inherited disease. Little is known, however, about the structural basis of pathogenic and clinically protective transthyretin mutants. Here we determined the solution structure of a transthyretin monomer that carries the clinically important T119M mutation. The structure displays a non-native arrangement that is distinct from all known structures of transthyretin and highlights the importance of high-resolution studies in solution for understanding molecular processes that lead to amyloid diseases.