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Structure paper

TitleStructural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation
Journal, issue, pagesSci Rep, Vol. 6, Page 21581-21581, Year 2016
Publish dateFeb 5, 2015 (structure data deposition date)
AuthorsChiang, C.H. / Grauffel, C. / Wu, L.S. / Kuo, P.H. / Doudeva, L.G. / Lim, C. / Shen, C.K. / Yuan, H.S.
External linksSci Rep / PubMed:26883171
MethodsX-ray diffraction
Resolution2.648 - 3 Å
Structure data

PDB-4y00:
Crystal Structure of Human TDP-43 RRM1 Domain with D169G Mutation in Complex with an Unmodified Single-stranded DNA
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4y0f:
Crystal Structure of Human TDP-43 RRM1 Domain in Complex with an Unmodified Single-stranded DNA
Method: X-RAY DIFFRACTION / Resolution: 2.648 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN/DNA / RNA recognition motif 1 Complex / DNA BINDING PROTEIN-DNA complex

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