5MDI
Crystal structure of TDP-43 N-terminal domain at 2.1 A resolution
Summary for 5MDI
Entry DOI | 10.2210/pdb5mdi/pdb |
Descriptor | TAR DNA-binding protein 43, ACETATE ION (3 entities in total) |
Functional Keywords | rna binding proteins, dynamic polymerization, als, protein aggregation, rna binding protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 22949.82 |
Authors | Afroz, T.,Hock, E.-M.,Ernst, P.,Foglieni, C.,Jambeau, M.,Gilhespy, L.,Laferriere, F.,Maniecka, Z.,Plueckthun, A.,Mittl, P.,Paganetti, P.,Allain, F.H.T.,Polymenidou, M. (deposition date: 2016-11-11, release date: 2017-07-05, Last modification date: 2017-07-12) |
Primary citation | Afroz, T.,Hock, E.M.,Ernst, P.,Foglieni, C.,Jambeau, M.,Gilhespy, L.A.B.,Laferriere, F.,Maniecka, Z.,Pluckthun, A.,Mittl, P.,Paganetti, P.,Allain, F.H.T.,Polymenidou, M. Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation. Nat Commun, 8:45-45, 2017 Cited by PubMed: 28663553DOI: 10.1038/s41467-017-00062-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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