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6EWW

Structure of 14-3-3 zeta in complex with CaMKK2 14-3-3 binding motif

Summary for 6EWW
Entry DOI10.2210/pdb6eww/pdb
Descriptor14-3-3 protein zeta/delta, ARG-LYS-LEU-SEP-LEU-GLN-GLU-ARG (3 entities in total)
Functional Keywords14-3-3 protein, calcium/calmodulin-dependent protein kinase kinase 2, camkk2, phosphorylation, signaling protein
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm : P63104
Total number of polymer chains8
Total formula weight110496.64
Authors
Lentini Santo, D.,Obsilova, V.,Obsil, T. (deposition date: 2017-11-06, release date: 2017-11-15, Last modification date: 2024-11-20)
Primary citationPsenakova, K.,Petrvalska, O.,Kylarova, S.,Lentini Santo, D.,Kalabova, D.,Herman, P.,Obsilova, V.,Obsil, T.
14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2).
Biochim. Biophys. Acta, 1862:1612-1625, 2018
Cited by
PubMed Abstract: Calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) is a member of the Ca/calmodulin-dependent kinase (CaMK) family involved in adiposity regulation, glucose homeostasis and cancer. This upstream activator of CaMKI, CaMKIV and AMP-activated protein kinase is inhibited by phosphorylation, which also triggers an association with the scaffolding protein 14-3-3. However, the role of 14-3-3 in the regulation of CaMKK2 remains unknown.
PubMed: 29649512
DOI: 10.1016/j.bbagen.2018.04.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.679 Å)
Structure validation

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