5FO2
Structure of human transthyretin mutant A108I
Summary for 5FO2
Entry DOI | 10.2210/pdb5fo2/pdb |
Descriptor | TRANSTHYRETIN (2 entities in total) |
Functional Keywords | transport protein, t4-binding protein non-amyloidogenic |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Secreted: P02766 |
Total number of polymer chains | 2 |
Total formula weight | 27638.88 |
Authors | Varejao, N.,Santanna, R.,Saraiva, M.J.,Gallego, P.,Ventura, S.,Reverter, D. (deposition date: 2015-11-17, release date: 2016-11-30, Last modification date: 2024-05-08) |
Primary citation | 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. Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation. Sci Rep, 7:44709-44709, 2017 Cited by PubMed: 28338000DOI: 10.1038/srep44709 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.449 Å) |
Structure validation
Download full validation report