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5MDI

Crystal structure of TDP-43 N-terminal domain at 2.1 A resolution

Summary for 5MDI
Entry DOI10.2210/pdb5mdi/pdb
DescriptorTAR DNA-binding protein 43, ACETATE ION (3 entities in total)
Functional Keywordsrna binding proteins, dynamic polymerization, als, protein aggregation, rna binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight22949.82
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 citationAfroz, 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: 28663553
DOI: 10.1038/s41467-017-00062-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

217705

数据于2024-03-27公开中

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