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; PubMed: 28338000; DOI: 10.1038/srep44709

Experimental method

X-RAY DIFFRACTION (1.449 Å)