Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation |
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Authors: | Dr. Jin Hae Kim Dr. Javier Oroz Prof. Dr. Markus Zweckstetter |
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Affiliation: | 1. Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), G?ttingen, Germany;2. Max-Planck-Institut für Biophysikalische Chemie, G?ttingen, Germany;3. Department of Neurology, University Medical Center G?ttingen, University of G?ttingen, G?ttingen, Germany |
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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. |
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Keywords: | NMR spectroscopy protein structures transthyretin |
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