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Structure paper

TitleKinase domain autophosphorylation rewires the activity and substrate specificity of CK1 enzymes.
Journal, issue, pagesMol. Cell, Vol. 82, Page 2006-, Year 2022
Publish dateJul 19, 2021 (structure data deposition date)
AuthorsCullati, S.N. / Chaikuad, A. / Chen, J.S. / Gebel, J. / Tesmer, L. / Zhubi, R. / Navarrete-Perea, J. / Guillen, R.X. / Gygi, S.P. / Hummer, G. ...Cullati, S.N. / Chaikuad, A. / Chen, J.S. / Gebel, J. / Tesmer, L. / Zhubi, R. / Navarrete-Perea, J. / Guillen, R.X. / Gygi, S.P. / Hummer, G. / Dotsch, V. / Knapp, S. / Gould, K.L.
External linksMol. Cell / PubMed:35353987
MethodsX-ray diffraction
Resolution1.7 - 2.4 Å
Structure data

PDB-7p7f:
Crystal structure of phosphorylated pT220 Casein Kinase I delta (CK1d), conformation 1
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-7p7g:
Crystal structure of phosphorylated pT220 Casein Kinase I delta (CK1d), conformation 2 and 3
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-7p7h:
Crystal structure of Casein Kinase I delta (CK1d) with alphaG-in conformation
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-ADN:
ADENOSINE

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / casein kinase / CK1d / CSNK1D / conformation plasticity / alpha G / activation segment / phosphorylation. / Structural Genomics / Structural Genomics Consortium / SGC / activation segment.

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