6T4B
CRYSTAL STRUCTURE OF HUMAN TDP-43 N-TERMINAL DOMAIN AT 2.55 A RESOLUTION
Summary for 6T4B
| Entry DOI | 10.2210/pdb6t4b/pdb |
| Descriptor | TAR DNA-binding protein 43, SULFATE ION (3 entities in total) |
| Functional Keywords | mnd, ntd domain, tdp-43, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 5 |
| Total formula weight | 44859.83 |
| Authors | Watanabe, T.F.,Wright, G.S.A.,Amporndanai, K.,Antonyuk, S.V.,Hasnain, S.S. (deposition date: 2019-10-13, release date: 2020-05-20, Last modification date: 2024-01-24) |
| Primary citation | Wright, G.S.A.,Watanabe, T.F.,Amporndanai, K.,Plotkin, S.S.,Cashman, N.R.,Antonyuk, S.V.,Hasnain, S.S. Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases. Iscience, 23:101159-101159, 2020 Cited by PubMed Abstract: Mislocalization, cleavage, and aggregation of the human protein TDP-43 is found in many neurodegenerative diseases. As is the case with many other proteins that are completely or partially structurally disordered, production of full-length recombinant TDP-43 in the quantities necessary for structural characterization has proved difficult. We show that the full-length TDP-43 protein and two truncated N-terminal constructs 1-270 and 1-263 can be heterologously expressed in E. coli. Full-length TDP-43 could be prevented from aggregation during purification using a detergent. Crystals grown from an N-terminal construct (1-270) revealed only the N-terminal domain (residues 1-80) with molecules arranged as parallel spirals with neighboring molecules arranged in head-to-tail fashion. To obtain detergent-free, full-length TDP-43 we mutated all six tryptophan residues to alanine. This provided sufficient soluble protein to collect small-angle X-ray scattering data. Refining relative positions of individual domains and intrinsically disordered regions against this data yielded a model of full-length TDP-43. PubMed: 32480125DOI: 10.1016/j.isci.2020.101159 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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