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TitleCrystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.
Journal, issue, pagesPlos One, Vol. 9, Page e103638-e103638, Year 2014
Publish dateFeb 13, 2014 (structure data deposition date)
AuthorsChamberlain, P. / Delker, S. / Pagarigan, B. / Mahmoudi, A. / Jackson, P. / Abbasian, M. / Muir, J. / Raheja, N. / Cathers, B.
External linksPlos One / PubMed:25111382
MethodsX-ray diffraction
Resolution1.8 - 2.6 Å
Structure data

PDB-4otd:
Crystal Structure of PRK1 Catalytic Domain
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4otg:
Crystal Structure of PRK1 Catalytic Domain in Complex with Lestaurtinib
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4oth:
Crystal Structure of PRK1 Catalytic Domain in Complex with Ro-31-8220
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4oti:
Crystal Structure of PRK1 Catalytic Domain in Complex with Tofacitinib
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-2V9:
Lestaurtinib

ChemComp-DRN:
BISINDOLYLMALEIMIDE IX

ChemComp-MI1:
3-{(3R,4R)-4-methyl-3-[methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]piperidin-1-yl}-3-oxopropanenitrile

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PRK1 / PKN1 / Protein kinase C related kinase 1 / KINASE / Protein Kinase / ATP Binding / Phosphorylation / TRANSFERASE/TRANSFERASE INHIBITOR / TRANSFERASE-TRANSFERASE INHIBITOR complex

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