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TitleA domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation.
Journal, issue, pagesNat Commun, Vol. 16, Page 8461-8461, Year 2025
Publish dateOct 28, 2023 (structure data deposition date)
AuthorsNguyen, B.V. / Ozden, C. / Dong, K. / Koc, O.C. / Torres-Ocampo, A.P. / Dziedzic, N. / Flaherty, D. / Huang, J. / Sankara, S. / Abromson, N.L. ...Nguyen, B.V. / Ozden, C. / Dong, K. / Koc, O.C. / Torres-Ocampo, A.P. / Dziedzic, N. / Flaherty, D. / Huang, J. / Sankara, S. / Abromson, N.L. / Tomchick, D.R. / Fissore, R.A. / Chen, J. / Garman, S.C. / Stratton, M.M.
External linksNat Commun / PubMed:41006217
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-8uso:
Full-length human CaMKII delta holoenzyme
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-MLI:
MALONATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / CaMKII / Kinase / CAMK2D / Holoenzyme

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