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Structure paper

TitleAn Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases.
Journal, issue, pagesJ. Med. Chem., Vol. 59, Page 10315-10321, Year 2016
Publish dateSep 20, 2016 (structure data deposition date)
AuthorsChaikuad, A. / Diharce, J. / Schroder, M. / Foucourt, A. / Leblond, B. / Casagrande, A.S. / Desire, L. / Bonnet, P. / Knapp, S. / Besson, T.
External linksJ. Med. Chem. / PubMed:27766861
MethodsX-ray diffraction
Resolution2.15 - 2.58 Å
Structure data

PDB-5lxc:
Crystal structure of DYRK2 in complex with EHT 5372 (Compound 1)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-5lxd:
Crystal structure of DYRK2 in complex with EHT 1610 (compound 2)
Method: X-RAY DIFFRACTION / Resolution: 2.58 Å

Chemicals

ChemComp-7AA:
methyl 9-[(2,4-dichlorophenyl)amino]-[1,3]thiazolo[5,4-f]quinazoline-2-carboximidate

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-7A7:
methyl 9-[(2-fluoranyl-4-methoxy-phenyl)amino]-[1,3]thiazolo[5,4-f]quinazoline-2-carboximidate

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / kinase / inhibitor / unusual binding mode / Structural Genomics / Structural Genomics Consortium / SGC

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