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Structure paper

TitleUnveiling the dimer/monomer propensities of Smad MH1-DNA complexes.
Journal, issue, pagesComput Struct Biotechnol J, Vol. 19, Page 632-646, Year 2021
Publish dateNov 4, 2019 (structure data deposition date)
AuthorsRuiz, L. / Kaczmarska, Z. / Gomes, T. / Aragon, E. / Torner, C. / Freier, R. / Baginski, B. / Martin-Malpartida, P. / de Martin Garrido, N. / Marquez, J.A. ...Ruiz, L. / Kaczmarska, Z. / Gomes, T. / Aragon, E. / Torner, C. / Freier, R. / Baginski, B. / Martin-Malpartida, P. / de Martin Garrido, N. / Marquez, J.A. / Cordeiro, T.N. / Pluta, R. / Macias, M.J.
External linksComput Struct Biotechnol J / PubMed:33510867
MethodsX-ray diffraction
Resolution1.782 - 2.92 Å
Structure data

PDB-6tbz:
Crystal structure of the MH1 domain of Smad5-Smad3 chimera construct bound to the GGCGC site
Method: X-RAY DIFFRACTION / Resolution: 1.782 Å

PDB-6tce:
Crystal structure of the GGCT site-bound MH1 domain of Smad5 containing a GGGS insertion in the Loop1
Method: X-RAY DIFFRACTION / Resolution: 2.92 Å

PDB-6zmn:
Crystal structure of the Smad3-Smad5 MH1 domain chimera bound to the GGCGC site
Method: X-RAY DIFFRACTION / Resolution: 2.333 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / TGF-B / SIGNALING PROTEIN / Smad3 / TGFbeta / dimerization / hinge loop / protein engineering

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