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Structure paper

TitleMultiple conformational states of the HPK1 kinase domain in complex with sunitinib reveal the structural changes accompanying HPK1 trans-regulation.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 9029-9036, Year 2019
Publish dateDec 21, 2018 (structure data deposition date)
AuthorsJohnson, E. / McTigue, M. / Gallego, R.A. / Johnson, T.W. / Timofeevski, S. / Maestre, M. / Fisher, T.S. / Kania, R. / Sawasdikosol, S. / Burakoff, S. / Cronin, C.N.
External linksJ. Biol. Chem. / PubMed:31018963
MethodsX-ray diffraction
Resolution2.05 - 2.966 Å
Structure data

PDB-6nfy:
Crystal structure of nonphosphorylated, HPK1 kinase domain in complex with sunitinib in the inactive state.
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-6nfz:
Crystal structure of diphosphorylated HPK1 kinase domain in complex with sunitinib in the active state.
Method: X-RAY DIFFRACTION / Resolution: 2.966 Å

PDB-6ng0:
Crystal structure of HPK1 kinase domain T165E,S171E phosphomimetic mutant in complex with sunitinib in the inactive state.
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-B49:
N-[2-(diethylamino)ethyl]-5-[(Z)-(5-fluoro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carbo

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Kinase / 3D domain swap / active state / SIGNALING PROTEIN / dimer / inactive state

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