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Structure paper

TitleFunctional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.
Journal, issue, pagesNat Commun, Vol. 8, Page 45-45, Year 2017
Publish dateNov 11, 2016 (structure data deposition date)
AuthorsAfroz, T. / Hock, E.M. / Ernst, P. / Foglieni, C. / Jambeau, M. / Gilhespy, L.A.B. / Laferriere, F. / Maniecka, Z. / Pluckthun, A. / Mittl, P. ...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.
External linksNat Commun / PubMed:28663553
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-5mdi:
Crystal structure of TDP-43 N-terminal domain at 2.1 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / RNA binding proteins / Dynamic polymerization / ALS / protein aggregation

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