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5FW6

Structure of human transthyretin mutant A108V

Summary for 5FW6
Entry DOI10.2210/pdb5fw6/pdb
Related5FW7 5FW8 5FW9 5FWB 5FWC
DescriptorTRANSTHYRETIN (2 entities in total)
Functional Keywordstransport protein, trasnport protein, t4-binding, t4-binding protein non-amyloidogenic
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationSecreted: P02766
Total number of polymer chains2
Total formula weight27610.83
Authors
Gallego, P.,Varejao, N.,Santanna, R.,Saraiva, M.J.,Ventura, S.,Reverter, D. (deposition date: 2016-02-12, release date: 2017-03-08, Last modification date: 2017-06-14)
Primary citationSant'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: 28338000
DOI: 10.1038/srep44709
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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