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Structure paper

TitleStructure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association.
Journal, issue, pagesSci Rep, Vol. 9, Page 54-54, Year 2019
Publish dateMar 9, 2018 (structure data deposition date)
AuthorsKukuk, L. / Dingley, A.J. / Granzin, J. / Nagel-Steger, L. / Thiagarajan-Rosenkranz, P. / Ciupka, D. / Hanel, K. / Batra-Safferling, R. / Pacheco, V. / Stoldt, M. ...Kukuk, L. / Dingley, A.J. / Granzin, J. / Nagel-Steger, L. / Thiagarajan-Rosenkranz, P. / Ciupka, D. / Hanel, K. / Batra-Safferling, R. / Pacheco, V. / Stoldt, M. / Pfeffer, K. / Beer-Hammer, S. / Willbold, D. / Koenig, B.W.
External linksSci Rep / PubMed:30631134
MethodsX-ray diffraction / NMR (solution)
Resolution2.05 Å
Structure data

PDB-6fxf:
Crystal structure of the SAM domain of murine SLy1
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-6g8o:
Solution structure of the cross-linked SAM domain dimer of murine SLy1
Method: SOLUTION NMR

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / SLy1 / SAM / adapter protein / scaffold protein

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