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TitleMechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 25, Page 591-600, Year 2018
Publish dateMar 10, 2018 (structure data deposition date)
AuthorsBotuyan, M.V. / Cui, G. / Drane, P. / Oliveira, C. / Detappe, A. / Brault, M.E. / Parnandi, N. / Chaubey, S. / Thompson, J.R. / Bragantini, B. ...Botuyan, M.V. / Cui, G. / Drane, P. / Oliveira, C. / Detappe, A. / Brault, M.E. / Parnandi, N. / Chaubey, S. / Thompson, J.R. / Bragantini, B. / Zhao, D. / Chapman, J.R. / Chowdhury, D. / Mer, G.
External linksNat. Struct. Mol. Biol. / PubMed:29967538
MethodsX-ray diffraction
Resolution1.97 - 2.49 Å
Structure data

PDB-6co1:
Structure of human TIRR in complex with 53BP1 Tudor domains
Method: X-RAY DIFFRACTION / Resolution: 2.179 Å

PDB-6co2:
Structure of an engineered protein (NUDT16TI) in complex with 53BP1 Tudor domains
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

PDB-6d0l:
Structure of human TIRR
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / DNA damage response / DNA repair / DNA damage signaling / 53BP1 / TIRR / NUDT16L1 / Designer protein / Engineered protein / NUDT16TI / NUDT16 / Tudor domain / RNA binding / RNA nucleotide diphosphatase / DNA double-strand break repair

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