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TitleDeath-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites
Journal, issue, pagesStructure, Year 2016
Publish dateFeb 4, 2005 (structure data deposition date)
AuthorsSimon, B. / Huart, A.S. / Temmerman, K. / Vahokoski, J. / Mertens, H.D. / Komadina, D. / Hoffmann, J.E. / Yumerefendi, H. / Svergun, D.I. / Kursula, P. ...Simon, B. / Huart, A.S. / Temmerman, K. / Vahokoski, J. / Mertens, H.D. / Komadina, D. / Hoffmann, J.E. / Yumerefendi, H. / Svergun, D.I. / Kursula, P. / Schultz, C. / McCarthy, A.A. / Hart, D.J. / Wilmanns, M.
External linksStructure / PubMed:27133022
MethodsX-ray diffraction
Resolution1.47 - 3.1 Å
Structure data

PDB-1yrp:
Catalytic domain of human ZIP kinase phosphorylated at Thr265
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-2a2a:
High-resolution crystallographic analysis of the autoinhibited conformation of a human death-associated protein kinase
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

PDB-2xzs:
Death associated protein kinase 1 residues 1-312
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-DTT:
2,3-DIHYDROXY-1,4-DITHIOBUTANE

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / kinase fold / phosphothreonine / protein kinase / autoinhibition / CALMODULIN / ESPRIT

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